Major allergen from Amaranthus palmeri pollen is a profilin: Isolation, partial characterisation and IgE recognition

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Lane 1: Dogfish; lane 2: Shark; lane 3: Megrim; lane 4: Hake; lane 5: Sole; lane 6: Cod; lane 7: Anchovy; lane 8: Tuna." ] ] ] "autores" => array:1 [ 0 => array:2 [ "autoresLista" => "S. Calderon-Rodriguez, F. Pineda, R. Perez, C. Muñoz" "autores" => array:4 [ 0 => array:2 [ "nombre" => "S." "apellidos" => "Calderon-Rodriguez" ] 1 => array:2 [ "nombre" => "F." "apellidos" => "Pineda" ] 2 => array:2 [ "nombre" => "R." "apellidos" => "Perez" ] 3 => array:2 [ "nombre" => "C." 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Mice were sensitised with OVA by intraperitoneal injection (i.p.) at Days 0, 14 and 28, followed by challenge with OVA inhalation at Days 31 and 34 after grouping. Values are means±SEM (n=13–15). Values at the same experimental point not sharing a common small letter are significantly different (P<0.05) from each other assayed using one-way ANOVA, followed by Duncan's new multiple range tests. E.U.=(Asample−Ablank)/(Apositive−Ablank); NSC, non-sensitised control; DC, dietary control. Serum dilution: 1:100 for IgE detection, 1:2000 for IgG2a detection and 1:3,000,000 for IgG1 detection. Some standard errors were too small to be depicted in the figure." ] ] ] "autores" => array:1 [ 0 => array:2 [ "autoresLista" => "C.-M. Ku, J.-Y. Lin" "autores" => array:2 [ 0 => array:2 [ "nombre" => "C.-M." "apellidos" => "Ku" ] 1 => array:2 [ "nombre" => "J.-Y." "apellidos" => "Lin" ] ] ] ] ] "idiomaDefecto" => "en" "EPUB" => "https://multimedia.elsevier.es/PublicationsMultimediaV1/item/epub/S0301054615001056?idApp=UINPBA00004N" "url" => "/03010546/0000004400000002/v1_201603070011/S0301054615001056/v1_201603070011/en/main.assets" ] "en" => array:19 [ "idiomaDefecto" => true "cabecera" => "Original Article" "titulo" => "Major allergen from Amaranthus palmeri pollen is a profilin: Isolation, partial characterisation and IgE recognition" "tieneTextoCompleto" => true "paginas" => array:1 [ 0 => array:2 [ "paginaInicial" => "160" "paginaFinal" => "166" ] ] "autores" => array:1 [ 0 => array:4 [ "autoresLista" => "C.M. Landa-Pineda, A. Arroyo-Becerra, A. Rosas-Alvarado, L.M. Terán, M.L. Garcia-Cruz, L.A. Marchat, C.A. Reyes-López" "autores" => array:7 [ 0 => array:3 [ "nombre" => "C.M." "apellidos" => "Landa-Pineda" "referencia" => array:1 [ 0 => array:2 [ "etiqueta" => "a" "identificador" => "aff0005" ] ] ] 1 => array:3 [ "nombre" => "A." "apellidos" => "Arroyo-Becerra" "referencia" => array:1 [ 0 => array:2 [ "etiqueta" => "b" "identificador" => "aff0010" ] ] ] 2 => array:3 [ "nombre" => "A." "apellidos" => "Rosas-Alvarado" "referencia" => array:1 [ 0 => array:2 [ "etiqueta" => "c" "identificador" => "aff0015" ] ] ] 3 => array:3 [ "nombre" => "L.M." "apellidos" => "Terán" "referencia" => array:1 [ 0 => array:2 [ "etiqueta" => "d" "identificador" => "aff0020" ] ] ] 4 => array:3 [ "nombre" => "M.L." "apellidos" => "Garcia-Cruz" "referencia" => array:1 [ 0 => array:2 [ "etiqueta" => "d" "identificador" => "aff0020" ] ] ] 5 => array:4 [ "nombre" => "L.A." "apellidos" => "Marchat" "email" => array:1 [ 0 => "lmarchat@gmail.com" ] "referencia" => array:2 [ 0 => array:2 [ "etiqueta" => "a" "identificador" => "aff0005" ] 1 => array:2 [ "etiqueta" => "*" "identificador" => "cor0005" ] ] ] 6 => array:4 [ "nombre" => "C.A." "apellidos" => "Reyes-López" "email" => array:1 [ 0 => "careyes@ipn.mx" ] "referencia" => array:2 [ 0 => array:2 [ "etiqueta" => "a" "identificador" => "aff0005" ] 1 => array:2 [ "etiqueta" => "*" "identificador" => "cor0005" ] ] ] ] "afiliaciones" => array:4 [ 0 => array:3 [ "entidad" => "Sección de Estudios de Posgrado e Investigación, ENMyH, IPN, México" "etiqueta" => "a" "identificador" => "aff0005" ] 1 => array:3 [ "entidad" => "CIBA, IPN, México" "etiqueta" => "b" "identificador" => "aff0010" ] 2 => array:3 [ "entidad" => "Servicio de Alergia e Inmunología Clínica, HGM, México" "etiqueta" => "c" "identificador" => "aff0015" ] 3 => array:3 [ "entidad" => "Departamento de Inmunogenética y Alergia, INER, México" "etiqueta" => "d" "identificador" => "aff0020" ] ] "correspondencia" => array:1 [ 0 => array:3 [ "identificador" => "cor0005" "etiqueta" => "⁎" "correspondencia" => "Corresponding authors." ] ] ] ] "resumenGrafico" => array:2 [ "original" => 0 "multimedia" => array:7 [ "identificador" => "fig0020" "etiqueta" => "Figure 4" "tipo" => "MULTIMEDIAFIGURA" "mostrarFloat" => true "mostrarDisplay" => false "figura" => array:1 [ 0 => array:4 [ "imagen" => "gr4.jpeg" "Alto" => 1142 "Ancho" => 1599 "Tamanyo" => 84594 ] ] "descripcion" => array:1 [ "en" => "IgE recognition of profilin by individual sera from patients hypersensitive to A. palmeri pollen. ELISA assay responses for sera of 15 patients. A pool of five non-allergic subject serum was used as controls (Ctrls−). A sample was considered positive when the OD450 value was higher than the mean value obtained for skin prick test negative people plus three standard deviations. The error bars indicate the standard deviation between ELISA replicates." ] ] ] "textoCompleto" => "IntroductionAllergy represents the most prevalent human disorder, affecting almost 30% of the population in developed and developing countries.<a class="elsevierStyleCrossRef" href="#bib0205">1</a> Allergic diseases include rhinoconjunctivitis, allergic asthma, and allergic dermatitis.<a class="elsevierStyleCrossRefs" href="#bib0205">1,2</a> Allergic tissue inflammation can be mitigated by anti-inflammatory drugs and immunosuppressive agents, however, only allergen-specific immunotherapy is considered as an effective and efficient treatment, with long-lasting clinical effects and can prevent the progression of mild forms of allergy to severe manifestations.<a class="elsevierStyleCrossRef" href="#bib0215">3</a> Recently, genetically engineered hypoallergenic derivatives have been incorporated to desensitisation immunotherapy.<a class="elsevierStyleCrossRef" href="#bib0220">4</a> This strategy requires detailed molecular and immunological studies to identify and design hypoallergenic molecules that can be used in allergen-specific immunotherapy.<a class="elsevierStyleCrossRef" href="#bib0215">3</a>Recent reports indicate that around half of allergic people present reactions to pollen allergens from different plants.<a class="elsevierStyleCrossRef" href="#bib0225">5</a> Furthermore, pollen-allergic patients frequently exhibit allergic symptoms after the ingestion of several kinds of plant-derived foods. This might be simply attributed to poly-sensitisation to different allergenic plants.<a class="elsevierStyleCrossRef" href="#bib0230">6</a> Another explanation for this phenomenon is the concept of IgE cross-reactivity between functional and structural related allergens, which are known as panallergens.Panallergens are evolutionarily conserved, ubiquitous components of several complex sources of allergens, which usually act as minor allergens. However, their presence has important clinical implications in establishing the phenomenon of food-pollen cross-reactivity, in the interpretation of diagnostic tests and in the preparation of immunotherapy extracts.One of the most studied pollen and plant-derived food panallergens is profilin, a well-known ubiquitous cytoskeleton protein that is highly conserved among eukaryotic cells. Binding sites and interacting motifs for different substrates have been characterised in many profilins, including plant proteins. In addition, secondary and tertiary structures of all profilins so far elucidated are amazingly similar. Profilins are involved in different molecular and cellular processes through binding to actin monomers,<a class="elsevierStyleCrossRef" href="#bib0235">7</a> actin-related proteins (ARPs), poly-l-proline (pLp) stretches,<a class="elsevierStyleCrossRef" href="#bib0240">8</a> and phosphatidylinositol lipids.<a class="elsevierStyleCrossRef" href="#bib0245">9</a> Profilin was recognised as an allergen for the first time in birch pollen.<a class="elsevierStyleCrossRef" href="#bib0250">10</a> Then, it was described as a relevant allergen in plant-derived foods, principally celery, carrot, peach, pear, apple, potato, tomato and pumpkin seed, which suggests that profilins could be responsible, at least in part, for cross-reactions between different allergens sources.<a class="elsevierStyleCrossRefs" href="#bib0225">5,11</a>Different clinical studies show that Amaranthus palmeri pollen is an important allergen source in the USA, Thailand and Mexico.<a class="elsevierStyleCrossRefs" href="#bib0260">12–14</a> However, little is known about the clinically relevant allergens of this pollen.To gain insights into the allergens of A. palmeri pollen, in this work we performed the isolation and purification of a profilin from pollen grains and evaluated its allergenic proprieties. Our results allowed the identification of four profilin isoforms in A. palmeri pollen and demonstrated their recognition by IgE from sera of A. palmeri-allergic people.Materials and methodsThe study was approved by the Ethical Committee of the National School of Medicine and Homeopathy of National Polytechnic Institute, Mexico and was carried out in compliance with the guidelines of the Helsinki Declaration of 1975. Participants gave their written informed consent.Pollen extract preparationPollen from A. palmeri (purity higher than 95%), was purchased by Antígenos Allergomex Distribuidora S.A. de C.V., Pollen was defatted by repeated changes of ethanol-acetone and diethyl ether. Defatted pollen (1g) was suspended in 10mL of 50mM carbonate buffer (50mM Na2CO3-NaHCO3, 5mM EDTA and 0.5mM PMSF; pH 8.0) and shaken for 16h at 4°C. Pollen grains were separated by centrifugation at 10,000×g for 15min, the supernatant was filtered through a 0.22μm pore size PVDF membrane (Millipore) and dialysed against 50mM carbonate buffer pH 8.0. Total proteins in aqueous pollen extract were quantified using the BCA Protein Assay kit (Pierce, USA) and protein integrity was verified by SDS-PAGE.Chromatographic isolation of profilin isoformsProfilin isoforms were purified by affinity chromatography using a poly-l-proline-Sepharose support. Briefly, protein extract was applied to a home-made pLp-Sepharose support at a flow rate of 0.5mL/min. Unbound proteins were washed away with 50mM carbonate buffer (20 column volumes), and 1M guanidine hydrochloride (two volumes) in ultrapure water. Then, retained profilins were eluted with 4M guanidine hydrochloride and dialysed against 50mM carbonate buffer, pH 8.0. Finally, eluted proteins were fractionated through an anion exchange column (Mono Q™ GE Healthcare) coupled to a HPLC (1220 Infinity LC, Agilent Technologies) equilibrated with 50mM phosphate buffer, pH 7.4. Retained proteins were eluted with the same buffer containing 1M NaCl. Each fraction was analysed by 16% SDS-PAGE and Coomassie Blue staining to evaluate profilin homogeneity. Protein concentration was determined by the bicinchoninic acid method.Immunodetection of profilinA. palmeri pollen extract and profilin obtained from affinity-chromatography were separated by 16% SDS-PAGE and electro-transferred onto polyvinylidene difluoride (PVDF) membranes (Immobilon-P, Millipore) using standard methods. Membranes were completely dried to block unoccupied sites and prevent nonspecific binding of antibodies. Then, membranes were incubated at room temperature for two hours with a monoclonal antibody against Arabidopsis thaliana profilin (Sigma–Aldrich®) (1:3000 dilution). After washing with PBS-Tween 0.05%, membranes were incubated for 1h at room temperature with an anti-mouse-IgG-HRP antibody (BioLegend®) (1:5000 dilution). Finally, bound antibodies were detected using 3,3-diaminobenzidine (Sigma–Aldrich®) as substrate.Profilin-specific monoclonal antibody bindingThe main Mono Q fractions obtained from affinity chromatography fraction were analysed by ELISA. Briefly, immunoplates (Corning Inc.) were coated with 10μg of protein per well diluted in coating buffer (0.05M carbonate bicarbonate buffer pH 9.6). Plates were incubated overnight at 4°C, washed with PBS-Tween 0.25% and blocked with 5% blocking agent (BLOT-QuickBlocker®, Millipore) in PBS at 25°C for 2h. After washing with PBS-Tween solution, 100μl of a monoclonal antibody against A. thaliana profilin (1:5000 dilution) were added in each well and incubated for one hour at room temperature. Plates were washed again and incubated for 1h at room temperature with an anti-mouse-IgG-HRP antibody (1:5000 dilution). Chromogenic substrate was prepared by adding 50μl of a tetramethylbenzidine (TMB) solution (6mg/ml in dimethyl sulfoxide) and 1.5μl of 3% H2O2 to 2.5ml of 0.1M sodium acetate (pH 5.5) solution. One hundred microlitres of the chromogenic substrate were added to each well. After 15min of incubation in the dark, colour development was stopped by addition of 100μl of 2N H2SO4. Optical density was read at 450nm using an ELISA plate reader (Stat Fax 303+, Awareness Technology, Inc.).Profilin identification by mass spectrometryMono Q column fractions that were detected as positive in the ELISA experiment described above, were first analysed by automated Edman degradation on a gas-phase protein sequencer (LF 3000, Beckman Instruments, Irvine, CA, USA). Because this experiment failed to identify protein (see below), proteins were then identified by mass spectrometry. For this, other aliquots of Mono Q fractions were submitted to 16% SDS-PAGE and Coomassie blue staining. Bands corresponding to about 14kDa, which is the expected molecular weight for profilin, were manually excised from polyacrylamide gel with a sterile scalpel. Gel pieces were washed twice with 50% (v/v) acetonitrile in 25mM ammonium bicarbonate (pH 8.5) for 15min to remove Coomassie dye. After dehydration with 100% (v/v) acetonitrile for 10min at room temperature, gel pieces were vacuum-dried and rehydrated with sequencing-grade modified trypsin (Promega, Madison, WI, USA) in 25mM ammonium bicarbonate (pH 8.5) at 37°C overnight. Then, in-gel tryptic digested samples were separated by Capillary HPLC and analysed by Electrospray tandem mass spectrometry (ESI-MS/MS) using a 3200 Q TRAP hybrid tandem mass spectrometer (Applied Biosystems/MDS Sciex, Concord, ON, Canada). Peptide mass and sequence were established from MS data and MS/MS fragmentation patterns of the peptides. Protein identification was performed by searching a non-redundant protein sequence database (NCBI) restricted to green plants using the Mascot search engine (<a id="intr0005" class="elsevierStyleInterRef" href="http://www.matrixscience.com/">http://www.matrixscience.com</a>).Detection of IgE against A. palmeri profilin by ELISAThe presence of specific-IgE that recognise A. palmeri profilins was evaluated by ELISA in serum of 15 allergic people with pollinosis, manifested by disease history and positive skin prick test (SPT) to A. palmeri pollen extract and other pollens. Five subjects with negative SPT responses were used as negative controls. Briefly, immunoplates were coated with purified profilin as described above. Wells were then incubated with patients’ serum (1:10 in PBS-Tween 0.05%) for 3h at 25°C and 15h at 4°C. After washing, biotinylated anti-human IgE (Zymed®) was added to each well (1:4000) and incubated for 2h at 25°C. The immunoplate was washed and incubated for 2h with streptavidin-horseradish peroxidase conjugate (Zymed®) at room temperature. Enzymatic reaction was detected using tetramethylbenzidine as substrate; the reaction was stopped with 2N H2SO4 after 15min incubation at room temperature and optical density was read at 450nm (OD450). A sample was considered positive when the OD450 value was higher than the mean value obtained for SPT negative people plus three standard deviations.ResultsA. palmeri pollen has a protein fraction that was recognised by an anti-profilin monoclonal antibodySDS-PAGE analysis of A. palmeri pollen extract revealed the presence of several proteins with molecular masses ranging from 12 to 75kDa (<a class="elsevierStyleCrossRef" href="#fig0005">Fig. 1</a>A). Interestingly, profilin-specific monoclonal antibody immunodetected a unique band with a molecular mass of 14kDa, which probably corresponds to A. palmeri profilin (<a class="elsevierStyleCrossRef" href="#fig0005">Fig. 1</a>A). Because profilins have conserved binding sites for poly-l-proline (pLp), we purified this allergen from A. palmeri pollen by affinity chromatography using a pLp-Sheparose column. Proteins with pLp affinity were obtained in a single elution fraction (<a class="elsevierStyleCrossRef" href="#fig0005">Fig. 1</a>C) with a yield of 150μg per gram of A. palmeri pollen processed. SDS-PAGE analysis confirmed the presence of a predominant band of about 14kDa, which corresponds to the expected molecular weight for profilin (<a class="elsevierStyleCrossRef" href="#fig0005">Fig. 1</a>B). Notably, this band was immunodetected by a monoclonal antibody against profilin from A. thaliana, which strongly suggests the presence of homologous proteins in this fraction (<a class="elsevierStyleCrossRef" href="#fig0005">Fig. 1</a>B).<elsevierMultimedia ident="fig0005"></elsevierMultimedia>A. palmeri pollen has at least four profilin isoformsProteins retained in pLp-Sepharose column were then submitted to anionic-exchange chromatography using a Mono Q column. Results evidenced the separation of seven main fractions (<a class="elsevierStyleCrossRef" href="#fig0010">Fig. 2</a>A). Notably, fractions F2–F5 were recognised by a monoclonal antibody against profilin from A. thaliana pollen in ELISA (<a class="elsevierStyleCrossRef" href="#fig0010">Fig. 2</a>B). Altogether, these results indicate the presence of at least four profilin isoforms in A. palmeri pollen extract.<elsevierMultimedia ident="fig0010"></elsevierMultimedia>Only fractions F4 and F5 were submitted to mass spectrometry analysis, because fractions F2 and F3 were insoluble proteins. In both fractions, mass spectrometry analysis identified two peptides that correspond to the sequence of profilin from other plants. Particularly, peptide 1 (YMVIQGEPGAVIR) totally matches with amino acids 72–84 in profilin from Hevea brasiliensis, while peptide 2 (LGDYLLDQGL) corresponds to the 122–131 amino acids region of the same protein. Moreover, regions corresponding to both peptides are highly conserved among allergenic profilins obtained from the allergome database (<a id="intr0010" class="elsevierStyleInterRef" href="http://www.allergome.org/">http://www.allergome.org/</a>) and aligned with clustal-W software (<a class="elsevierStyleCrossRef" href="#fig0015">Fig. 3</a>).<elsevierMultimedia ident="fig0015"></elsevierMultimedia>A. palmeri profilin is a relevant allergenPatients’ characteristics and sensitisation profiles are summarised in <a class="elsevierStyleCrossRef" href="#tbl0005">Table 1</a>. Respiratory symptoms of rhinitis were reported in 12 of 15 patients (80%) and rhinitis and asthma symptoms were reported in three of 15 (20%) patients. No food allergy symptoms were reported in any patient. High prevalence of sensitisation to Fraxinus excelsior, Ligustrum vulgare, Chenopodium album and Atriplex stocksii pollen were reported in patients with positive SPT to A. palmeri pollen.<elsevierMultimedia ident="tbl0005"></elsevierMultimedia>In order to evaluate the allergenicity of A. palmeri pollen profilin, we analysed serum from 15 individual patients’ with positive SPT to A. palmeri pollen extract by ELISA, using the profilins contained in the fraction obtained from affinity chromatography as antigen. Result showed that 9 out of 15 sera contain specific IgE antibodies that recognised profilins coated in wells, representing 60% of the sera tested (<a class="elsevierStyleCrossRef" href="#fig0020">Fig. 4</a>).<elsevierMultimedia ident="fig0020"></elsevierMultimedia>DiscussionBecause of the high amino acid sequence identity between profilins from different organisms and consequently their comparable immunogenicity, profilins have been described as pan-allergens of various plant species.<a class="elsevierStyleCrossRef" href="#bib0275">15</a> In this study, the identification of profilin from A. palmeri pollen and the presence of profilin-specific IgE antibodies in serum of patients is reported. In A. palmeri, at least four profilin isoforms are expressed in pollen, as demonstrated by anion-exchange chromatography and ELISA using a monoclonal antibody against A. thaliana pollen profilin. Similarly, several isoforms have been reported for allergenic profilin from pollen of Ambrosia artemisiifolia (isoforms Amb a 8.01 and Amb a 8.02),<a class="elsevierStyleCrossRef" href="#bib0280">16</a>Amaranthus viridis (Ama v 2.0101 and Ama v 2.0201),<a class="elsevierStyleCrossRef" href="#bib0285">17</a>Phleum pratense (Phl p 12.0101, Phl p 12.0102, Phl p 12.0103),<a class="elsevierStyleCrossRef" href="#bib0290">18</a>Salsola kali (Sal k 4.0101, Sal k 4.0201, Sal k 4.0301),<a class="elsevierStyleCrossRef" href="#bib0295">19</a> among other pollens. Purification yield of profilin by affinity chromatography was 150μg/g of pollen, slightly higher than previously reported for other pollens using similar purification protocols, such as sunflower, olive and lambsquarters, which showed yields between 30 and 100μg/g of pollen.<a class="elsevierStyleCrossRefs" href="#bib0300">20–23</a> Moreover, purity of profilin after anion-exchange chromatography was more than 95% according to SDS-PAGE and colloidal Coomassie Blue staining.Fractions (F4 and F5) from anion-exchange chromatography containing profilin isoforms were initially subjected to automated Edman sequencing; however assays failed to release a NH2-terminal residue from these fractions (data not shown). These results suggested the presence of a possible post-translational modification of profilin from A. palmeri pollen. NH2-terminal blockage typically occurs when the α-amino groups are acylated or when the N-terminal residue is a pyrrolidone carboxylic acid formed by cyclisation of glutamine.<a class="elsevierStyleCrossRef" href="#bib0320">24</a> Proteins with serine and alanine termini are the most frequently acetylated, plant profilins display a very high degree of amino acid sequence homology in N-terminal segment (residues 1–15).<a class="elsevierStyleCrossRefs" href="#bib0315">23,25,26</a> Importantly, serine 2 is present in all reported sequences of allergenic profilins from pollen, which reinforced the idea that a post-translational modification is present in A. palmeri pollen profilin isoforms, most likely, an acetylation of the N-terminal serine. Allergenic profilins with blocked N-terminal amino acid have also been reported in melon<a class="elsevierStyleCrossRef" href="#bib0330">26</a> and olive pollen.<a class="elsevierStyleCrossRef" href="#bib0335">27</a> This N-terminal modification has also been identified in other plant allergens, such as lipid transfer protein from peach<a class="elsevierStyleCrossRef" href="#bib0340">28</a> and isoflavone reductase from birch pollen.<a class="elsevierStyleCrossRef" href="#bib0345">29</a> Because it was not possible to obtain the N-terminal sequence of amino acids from isolated profilin isoforms through Edman degradation method, we performed their identification by mass spectrometry. The detection of two peptides that showed highly conserved amino acid sequence found in profilins from allergenic pollen of a large number of plants, confirmed the identification of profilin isoforms in A. palmeri. Identified peptides are contained in a region that has been previously reported as part of a major IgE binding-site in profilins from H. brasiliensis, Betula pendula, and A. thaliana.<a class="elsevierStyleCrossRef" href="#bib0350">30</a> Preliminary results obtained by our group show that profilin isoforms identified in this work have a molecular mass of 13,950Da for isoform present in F4 and of 13,958Da for profilin in F5, as judged by MALDI-TOF mass spectrometry analysis (data no shown), which is consistent with the expected molecular mass for these proteins. This result reinforces earlier evidence that identified allergen belongs to profilin family.On the other hand, ELISA analysis revealed that 60% of serum from patients with positive SPT to A. palmeri pollen showed specific IgE to pooled profilin isoforms. Similar sensitisation rates were observed in patients with positive SPT to F. excelsior pollen (53%). Slightly lower rates of sensitisation were observed in patients with positive SPT to L. vulgare and A. stocksii pollen (47%), suggesting a possible role of A. plameri profilin in cross-reactivity among these pollens. Interestingly, patients with positive SPT to C. album pollen, a plant of Amaranthaceae/Chenopodiaceae family, only 33% showed IgE to A. palmeri profilin. In contrary to our finding, previous reports showed sensitisation rates of 55% to profilin from C. album pollen in Spanish patients.<a class="elsevierStyleCrossRef" href="#bib0315">23</a> It is to note that profilin has been found to be a minor but important allergen in pollen from birch (20%), timothy (20%),<a class="elsevierStyleCrossRef" href="#bib0275">15</a> mugwort (20–36%),<a class="elsevierStyleCrossRefs" href="#bib0275">15,31</a> olive (24–47%)<a class="elsevierStyleCrossRefs" href="#bib0335">27,32</a> and sunflower (30%).<a class="elsevierStyleCrossRef" href="#bib0365">33</a> Nonetheless, it has been found to be a major allergen in other pollens, such as annual mercury (51%),<a class="elsevierStyleCrossRef" href="#bib0370">34</a> saffron (53%),<a class="elsevierStyleCrossRef" href="#bib0375">35</a> lambsquarters (55%),<a class="elsevierStyleCrossRef" href="#bib0315">23</a> date palm (56–64%),<a class="elsevierStyleCrossRef" href="#bib0380">36</a> and soybean (69%).<a class="elsevierStyleCrossRef" href="#bib0385">37</a> Similar observations have been reported for profilin of some plant food extract such as muskmelon (71–100%),<a class="elsevierStyleCrossRefs" href="#bib0330">26,38</a> orange (78–87%)<a class="elsevierStyleCrossRef" href="#bib0395">39</a> or watermelon, with a rate of profilin-sensitised patients of 56%.<a class="elsevierStyleCrossRef" href="#bib0400">40</a>In conclusion, we have demonstrated that profilin from A. palmeri pollen is an important allergen for Mexican allergic subjects, which suggests that it can be considered as a panallergen allergen in this allergenic source. Further studies are required to determine whether profilin isoforms represent interesting candidates to be included in desensitisation protocols for people allergic to A. palmeri pollen.Conflict of interestThe authors have no conflict of interest to declare.Ethical disclosuresConfidentiality of dataThe authors declare that they have followed the protocols of their work centre on the publication of patient data and that all the patients included in the study have received sufficient information and have given their informed consent in writing to participate in that study.Right to privacy and informed consentThe authors have obtained the informed consent of the patients and/or subjects mentioned in the article. The author for correspondence is in possession of this document.Protection of human subjects and animals in researchThe authors declare that the procedures followed were in accordance with the regulations of the responsible Clinical Research Ethics Committee and in accordance with those of the World Medical Association and the Helsinki Declaration." "textoCompletoSecciones" => array:1 [ "secciones" => array:10 [ 0 => array:3 [ "identificador" => "xres612835" "titulo" => "Abstract" "secciones" => array:4 [ 0 => array:2 [ "identificador" => "abst0005" "titulo" => "Background" ] 1 => array:2 [ "identificador" => "abst0010" "titulo" => "Methods" ] 2 => array:2 [ "identificador" => "abst0015" "titulo" => "Principal findings" ] 3 => array:2 [ "identificador" => "abst0020" "titulo" => "Conclusion" ] ] ] 1 => array:2 [ "identificador" => "xpalclavsec626628" "titulo" => "Keywords" ] 2 => array:2 [ "identificador" => "sec0005" "titulo" => "Introduction" ] 3 => array:3 [ "identificador" => "sec0010" "titulo" => "Materials and methods" "secciones" => array:6 [ 0 => array:2 [ "identificador" => "sec0015" "titulo" => "Pollen extract preparation" ] 1 => array:2 [ "identificador" => "sec0020" "titulo" => "Chromatographic isolation of profilin isoforms" ] 2 => array:2 [ "identificador" => "sec0025" "titulo" => "Immunodetection of profilin" ] 3 => array:2 [ "identificador" => "sec0030" "titulo" => "Profilin-specific monoclonal antibody binding" ] 4 => array:2 [ "identificador" => "sec0035" "titulo" => "Profilin identification by mass spectrometry" ] 5 => array:2 [ "identificador" => "sec0040" "titulo" => "Detection of IgE against A. palmeri profilin by ELISA" ] ] ] 4 => array:3 [ "identificador" => "sec0045" "titulo" => "Results" "secciones" => array:3 [ 0 => array:2 [ "identificador" => "sec0050" "titulo" => "A. palmeri pollen has a protein fraction that was recognised by an anti-profilin monoclonal antibody" ] 1 => array:2 [ "identificador" => "sec0055" "titulo" => "A. palmeri pollen has at least four profilin isoforms" ] 2 => array:2 [ "identificador" => "sec0060" "titulo" => "A. palmeri profilin is a relevant allergen" ] ] ] 5 => array:2 [ "identificador" => "sec0065" "titulo" => "Discussion" ] 6 => array:2 [ "identificador" => "sec0070" "titulo" => "Conflict of interest" ] 7 => array:3 [ "identificador" => "sec0075" "titulo" => "Ethical disclosures" "secciones" => array:3 [ 0 => array:2 [ "identificador" => "sec0080" "titulo" => "Confidentiality of data" ] 1 => array:2 [ "identificador" => "sec0085" "titulo" => "Right to privacy and informed consent" ] 2 => array:2 [ "identificador" => "sec0090" "titulo" => "Protection of human subjects and animals in research" ] ] ] 8 => array:2 [ "identificador" => "xack206569" "titulo" => "Acknowledgments" ] 9 => array:1 [ "titulo" => "References" ] ] ] "pdfFichero" => "main.pdf" "tienePdf" => true "fechaRecibido" => "2015-02-17" "fechaAceptado" => "2015-05-07" "PalabrasClave" => array:1 [ "en" => array:1 [ 0 => array:4 [ "clase" => "keyword" "titulo" => "Keywords" "identificador" => "xpalclavsec626628" "palabras" => array:4 [ 0 => "Allergen" 1 => "Amaranthus palmeri" 2 => "Pollen" 3 => "Profilin" ] ] ] ] "tieneResumen" => true "resumen" => array:1 [ "en" => array:3 [ "titulo" => "Abstract" "resumen" => "BackgroundPollens represent a rich source of proteins that are also potential elicitors of IgE-mediated pollen allergy. Sensitisation to panallergens could play an important role in diagnosis and specific immunotherapy, because these molecules are present in different plant pollens and plant foods and have marked structural similarity in different species. Profilins are one of the most common panallergens to be studied because they are responsible for a large number of sensitisations and are clearly related to cross-reactivity and co-sensitisation. This study aimed to isolate and characterise a new allergen of Amaranthus palmeri pollen and to determine its allergenicity. MethodsA. palmeri pollen profilin was purified using poly-l-proline-Sepharose affinity chromatography followed by anion exchanger chromatography. Identification of purified protein was carried out by mass spectrometry. Specific IgE was estimated in sera of patients with positive skin prick test to A. palmeri pollen extract, by enzyme-linked immunosorbent assay (ELISA). Principal findingsPurified protein appeared as a single band at 14kDa in SDS-PAGE gel. Mass spectrometric analysis of the gel band identified two highly conserved peptides corresponding to allergenic profilins from pollen of other plants. Sera from about 60% of allergic patients have IgE that recognises the purified A. palmeri protein. ConclusionA 14kDa protein of A. palmeri pollen was purified and identified as allergenic profilin, which was recognised by sera from pollen allergic patients." "secciones" => array:4 [ 0 => array:2 [ "identificador" => "abst0005" "titulo" => "Background" ] 1 => array:2 [ "identificador" => "abst0010" "titulo" => "Methods" ] 2 => array:2 [ "identificador" => "abst0015" "titulo" => "Principal findings" ] 3 => array:2 [ "identificador" => "abst0020" "titulo" => "Conclusion" ] ] ] ] "multimedia" => array:5 [ 0 => array:7 [ "identificador" => "fig0005" "etiqueta" => "Figure 1" "tipo" => "MULTIMEDIAFIGURA" "mostrarFloat" => true "mostrarDisplay" => false "figura" => array:1 [ 0 => array:4 [ "imagen" => "gr1.jpeg" "Alto" => 1487 "Ancho" => 3167 "Tamanyo" => 158842 ] ] "descripcion" => array:1 [ "en" => "Purification of profilin of A. palmeri pollen by Affinity chromatography. (A) SDS-PAGE of pollen extracts. Total and purified proteins were separated on 15% acrylamide gel and stained by colloidal Coomassie blue. Lane 1, molecular weight markers (kDa); lane 2, total protein extract; lane 3, purified proteins. (B) Immunodetection of profilin. Total and purified proteins were immunodetected by monoclonal antibody against profilin from A. thaliana. Lane 1, total protein extract; lane 2, purified proteins. (C) Elution profile of retained proteins from p-L-p-Sheparose column (arrow indicate addition of 4M of guanidine–HCl)." ] ] 1 => array:7 [ "identificador" => "fig0010" "etiqueta" => "Figure 2" "tipo" => "MULTIMEDIAFIGURA" "mostrarFloat" => true "mostrarDisplay" => false "figura" => array:1 [ 0 => array:4 [ "imagen" => "gr2.jpeg" "Alto" => 1239 "Ancho" => 3197 "Tamanyo" => 132205 ] ] "descripcion" => array:1 [ "en" => "Anion-exchange chromatography on Mono Q and ELISA assay. (A) Ion-exchange chromatography of profilin retained from affinity column. Solid line represents A280; segmented line represents salt gradient up to 1M NaCl. Major fractions are labelled F1–F7. (B) Fractions recognised by a monoclonal A. thaliana profilin antibody in ELISA. Antibody against A. thaliana profilin binding with no protein in wells was used as negative control (Ctrl−)." ] ] 2 => array:7 [ "identificador" => "fig0015" "etiqueta" => "Figure 3" "tipo" => "MULTIMEDIAFIGURA" "mostrarFloat" => true "mostrarDisplay" => false "figura" => array:1 [ 0 => array:4 [ "imagen" => "gr3.jpeg" "Alto" => 835 "Ancho" => 1541 "Tamanyo" => 198711 ] ] "descripcion" => array:1 [ "en" => "Comparison of identified A. palmeri peptide amino acid sequences with profilins from other allergenic sources. (A) Peptide 1 (internal peptide) and (B) peptide 2 (C-terminal peptide). Sequence identity (*) and amino acid changes with conserved physicochemical properties (:) of peptides identified in A. palmeri pollen profilin were identified through compared with sequences of profilins from highly allergenic sources from H. brasiliensis (CAA75312), A. retroflexus (ACP43298), A. viridis (ABW37744), P. pratense (Y09457) and B. verrucosa (P25816)." ] ] 3 => array:7 [ "identificador" => "fig0020" "etiqueta" => "Figure 4" "tipo" => "MULTIMEDIAFIGURA" "mostrarFloat" => true "mostrarDisplay" => false "figura" => array:1 [ 0 => array:4 [ "imagen" => "gr4.jpeg" "Alto" => 1142 "Ancho" => 1599 "Tamanyo" => 84594 ] ] "descripcion" => array:1 [ "en" => "IgE recognition of profilin by individual sera from patients hypersensitive to A. palmeri pollen. ELISA assay responses for sera of 15 patients. A pool of five non-allergic subject serum was used as controls (Ctrls−). A sample was considered positive when the OD450 value was higher than the mean value obtained for skin prick test negative people plus three standard deviations. The error bars indicate the standard deviation between ELISA replicates." ] ] 4 => array:7 [ "identificador" => "tbl0005" "etiqueta" => "Table 1" "tipo" => "MULTIMEDIATABLA" "mostrarFloat" => true "mostrarDisplay" => false "tabla" => array:2 [ "leyenda" => "Abbreviations: SPT (+), positive skin prick test." "tablatextoimagen" => array:1 [ 0 => array:2 [ "tabla" => array:1 [ 0 => """ <table border="0" frame="\n \t\t\t\t\tvoid\n \t\t\t\t" class=""><thead title="thead"><tr title="table-row"><th class="td" title="table-head " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Allergen source \t\t\t\t\t\t\n \t\t\t\t</th><th class="td" title="table-head " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Rhinitis (n/%) \t\t\t\t\t\t\n \t\t\t\t</th><th class="td" title="table-head " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Rhinitis and asthma (n/%) \t\t\t\t\t\t\n \t\t\t\t</th><th class="td" title="table-head " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">SPT (+) (n/%) \t\t\t\t\t\t\n \t\t\t\t</th><th class="td" title="table-head " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Specific IgE to A. palmeri profilin (n/%) \t\t\t\t\t\t\n \t\t\t\t</th></tr></thead><tbody title="tbody"><tr title="table-row"><td class="td" title="table-entry " align="left" valign="top">Amaranthus palmeri \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">12/80 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">3/20 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">15/100 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">9/60 \t\t\t\t\t\t\n \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry " align="left" valign="top">Fraxinus excelsior \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">11/73 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">2/13 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">12/80 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">8/53 \t\t\t\t\t\t\n \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry " align="left" valign="top">Ligustrum vulgare \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">10/66 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">3/20 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">13/87 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">7/47 \t\t\t\t\t\t\n \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry " align="left" valign="top">Chenopodium album \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">6/40 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">3/20 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">8/53 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">5/33 \t\t\t\t\t\t\n \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry " align="left" valign="top">Atriplex stocksii \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">7/47 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">2/13 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">9/60 \t\t\t\t\t\t\n \t\t\t\t</td><td class="td" title="table-entry " align="left" valign="top">7/47 \t\t\t\t\t\t\n \t\t\t\t</td></tr></tbody></table> """ ] "imagenFichero" => array:1 [ 0 => "xTab1003952.png" ] ] ] ] "descripcion" => array:1 [ "en" => "Sensitisation profiles as estimated by skin prick testing or specific immunoglobulin E determination." ] ] ] "bibliografia" => array:2 [ "titulo" => "References" "seccion" => array:1 [ 0 => array:2 [ "identificador" => "bibs0005" "bibliografiaReferencia" => array:40 [ 0 => array:3 [ "identificador" => "bib0205" "etiqueta" => "1" "referencia" => array:1 [ 0 => array:2 [ "contribucion" => array:1 [ 0 => array:2 [ "titulo" => "Too clean, or not too clean: the hygiene hypothesis and home hygiene" "autores" => array:1 [ 0 => array:2 [ "etal" => false "autores" => array:4 [ 0 => "S.F. 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Original Article

C.M. Landa-Pinedaa, A. Arroyo-Becerrab, A. Rosas-Alvaradoc, L.M. Teránd, M.L. Garcia-Cruzd, L.A. Marchata,

Corresponding author

lmarchat@gmail.com

Corresponding authors.

, C.A. Reyes-Lópeza,

Corresponding author

careyes@ipn.mx

Corresponding authors.

a Sección de Estudios de Posgrado e Investigación, ENMyH, IPN, México

b CIBA, IPN, México

c Servicio de Alergia e Inmunología Clínica, HGM, México

d Departamento de Inmunogenética y Alergia, INER, México

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          "en" => "<p id="spar0040" class="elsevierStyleSimplePara elsevierViewall">IgE recognition of profilin by individual sera from patients hypersensitive to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen&#46; ELISA assay responses for sera of 15 patients&#46; A pool of five non-allergic subject serum was used as controls &#40;Ctrls&#8722;&#41;&#46; A sample was considered positive when the OD<span class="elsevierStyleInf">450</span> value was higher than the mean value obtained for skin prick test negative people plus three standard deviations&#46; The error bars indicate the standard deviation between ELISA replicates&#46;</p>"
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    "textoCompleto" => "<span class="elsevierStyleSections"><span id="sec0005" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0035">Introduction</span><p id="par0005" class="elsevierStylePara elsevierViewall">Allergy represents the most prevalent human disorder&#44; affecting almost 30&#37; of the population in developed and developing countries&#46;<a class="elsevierStyleCrossRef" href="#bib0205"><span class="elsevierStyleSup">1</span></a> Allergic diseases include rhinoconjunctivitis&#44; allergic asthma&#44; and allergic dermatitis&#46;<a class="elsevierStyleCrossRefs" href="#bib0205"><span class="elsevierStyleSup">1&#44;2</span></a> Allergic tissue inflammation can be mitigated by anti-inflammatory drugs and immunosuppressive agents&#44; however&#44; only allergen-specific immunotherapy is considered as an effective and efficient treatment&#44; with long-lasting clinical effects and can prevent the progression of mild forms of allergy to severe manifestations&#46;<a class="elsevierStyleCrossRef" href="#bib0215"><span class="elsevierStyleSup">3</span></a> Recently&#44; genetically engineered hypoallergenic derivatives have been incorporated to desensitisation immunotherapy&#46;<a class="elsevierStyleCrossRef" href="#bib0220"><span class="elsevierStyleSup">4</span></a> This strategy requires detailed molecular and immunological studies to identify and design hypoallergenic molecules that can be used in allergen-specific immunotherapy&#46;<a class="elsevierStyleCrossRef" href="#bib0215"><span class="elsevierStyleSup">3</span></a></p><p id="par0010" class="elsevierStylePara elsevierViewall">Recent reports indicate that around half of allergic people present reactions to pollen allergens from different plants&#46;<a class="elsevierStyleCrossRef" href="#bib0225"><span class="elsevierStyleSup">5</span></a> Furthermore&#44; pollen-allergic patients frequently exhibit allergic symptoms after the ingestion of several kinds of plant-derived foods&#46; This might be simply attributed to poly-sensitisation to different allergenic plants&#46;<a class="elsevierStyleCrossRef" href="#bib0230"><span class="elsevierStyleSup">6</span></a> Another explanation for this phenomenon is the concept of IgE cross-reactivity between functional and structural related allergens&#44; which are known as panallergens&#46;</p><p id="par0015" class="elsevierStylePara elsevierViewall">Panallergens are evolutionarily conserved&#44; ubiquitous components of several complex sources of allergens&#44; which usually act as minor allergens&#46; However&#44; their presence has important clinical implications in establishing the phenomenon of food-pollen cross-reactivity&#44; in the interpretation of diagnostic tests and in the preparation of immunotherapy extracts&#46;</p><p id="par0020" class="elsevierStylePara elsevierViewall">One of the most studied pollen and plant-derived food panallergens is profilin&#44; a well-known ubiquitous cytoskeleton protein that is highly conserved among eukaryotic cells&#46; Binding sites and interacting motifs for different substrates have been characterised in many profilins&#44; including plant proteins&#46; In addition&#44; secondary and tertiary structures of all profilins so far elucidated are amazingly similar&#46; Profilins are involved in different molecular and cellular processes through binding to actin monomers&#44;<a class="elsevierStyleCrossRef" href="#bib0235"><span class="elsevierStyleSup">7</span></a> actin-related proteins &#40;ARPs&#41;&#44; poly-<span class="elsevierStyleSmallCaps">l</span>-proline &#40;pLp&#41; stretches&#44;<a class="elsevierStyleCrossRef" href="#bib0240"><span class="elsevierStyleSup">8</span></a> and phosphatidylinositol lipids&#46;<a class="elsevierStyleCrossRef" href="#bib0245"><span class="elsevierStyleSup">9</span></a> Profilin was recognised as an allergen for the first time in birch pollen&#46;<a class="elsevierStyleCrossRef" href="#bib0250"><span class="elsevierStyleSup">10</span></a> Then&#44; it was described as a relevant allergen in plant-derived foods&#44; principally celery&#44; carrot&#44; peach&#44; pear&#44; apple&#44; potato&#44; tomato and pumpkin seed&#44; which suggests that profilins could be responsible&#44; at least in part&#44; for cross-reactions between different allergens sources&#46;<a class="elsevierStyleCrossRefs" href="#bib0225"><span class="elsevierStyleSup">5&#44;11</span></a></p><p id="par0025" class="elsevierStylePara elsevierViewall">Different clinical studies show that <span class="elsevierStyleItalic">Amaranthus palmeri</span> pollen is an important allergen source in the USA&#44; Thailand and Mexico&#46;<a class="elsevierStyleCrossRefs" href="#bib0260"><span class="elsevierStyleSup">12&#8211;14</span></a> However&#44; little is known about the clinically relevant allergens of this pollen&#46;</p><p id="par0030" class="elsevierStylePara elsevierViewall">To gain insights into the allergens of <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen&#44; in this work we performed the isolation and purification of a profilin from pollen grains and evaluated its allergenic proprieties&#46; Our results allowed the identification of four profilin isoforms in <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen and demonstrated their recognition by IgE from sera of <span class="elsevierStyleItalic">A&#46; palmeri</span>-allergic people&#46;</p></span><span id="sec0010" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0040">Materials and methods</span><p id="par0035" class="elsevierStylePara elsevierViewall">The study was approved by the Ethical Committee of the National School of Medicine and Homeopathy of National Polytechnic Institute&#44; Mexico and was carried out in compliance with the guidelines of the Helsinki Declaration of 1975&#46; Participants gave their written informed consent&#46;</p><span id="sec0015" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0045">Pollen extract preparation</span><p id="par0040" class="elsevierStylePara elsevierViewall">Pollen from <span class="elsevierStyleItalic">A&#46; palmeri</span> &#40;purity higher than 95&#37;&#41;&#44; was purchased by <span class="elsevierStyleItalic">Ant&#237;genos Allergomex Distribuidora S&#46;A&#46; de C&#46;V</span>&#46;&#44; Pollen was defatted by repeated changes of ethanol-acetone and diethyl ether&#46; Defatted pollen &#40;1<span class="elsevierStyleHsp" style=""></span>g&#41; was suspended in 10<span class="elsevierStyleHsp" style=""></span>mL of 50<span class="elsevierStyleHsp" style=""></span>mM carbonate buffer &#40;50<span class="elsevierStyleHsp" style=""></span>mM Na<span class="elsevierStyleInf">2</span>CO<span class="elsevierStyleInf">3</span>-NaHCO<span class="elsevierStyleInf">3</span>&#44; 5<span class="elsevierStyleHsp" style=""></span>mM EDTA and 0&#46;5<span class="elsevierStyleHsp" style=""></span>mM PMSF&#59; pH 8&#46;0&#41; and shaken for 16<span class="elsevierStyleHsp" style=""></span>h at 4<span class="elsevierStyleHsp" style=""></span>&#176;C&#46; Pollen grains were separated by centrifugation at 10&#44;000<span class="elsevierStyleHsp" style=""></span>&#215;<span class="elsevierStyleHsp" style=""></span><span class="elsevierStyleItalic">g</span> for 15<span class="elsevierStyleHsp" style=""></span>min&#44; the supernatant was filtered through a 0&#46;22<span class="elsevierStyleHsp" style=""></span>&#956;m pore size PVDF membrane &#40;Millipore&#41; and dialysed against 50<span class="elsevierStyleHsp" style=""></span>mM carbonate buffer pH 8&#46;0&#46; Total proteins in aqueous pollen extract were quantified using the BCA Protein Assay kit &#40;Pierce&#44; USA&#41; and protein integrity was verified by SDS-PAGE&#46;</p></span><span id="sec0020" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0050">Chromatographic isolation of profilin isoforms</span><p id="par0045" class="elsevierStylePara elsevierViewall">Profilin isoforms were purified by affinity chromatography using a poly-<span class="elsevierStyleSmallCaps">l</span>-proline-Sepharose support&#46; Briefly&#44; protein extract was applied to a home-made pLp-Sepharose support at a flow rate of 0&#46;5<span class="elsevierStyleHsp" style=""></span>mL&#47;min&#46; Unbound proteins were washed away with 50<span class="elsevierStyleHsp" style=""></span>mM carbonate buffer &#40;20 column volumes&#41;&#44; and 1<span class="elsevierStyleHsp" style=""></span>M guanidine hydrochloride &#40;two volumes&#41; in ultrapure water&#46; Then&#44; retained profilins were eluted with 4<span class="elsevierStyleHsp" style=""></span>M guanidine hydrochloride and dialysed against 50<span class="elsevierStyleHsp" style=""></span>mM carbonate buffer&#44; pH 8&#46;0&#46; Finally&#44; eluted proteins were fractionated through an anion exchange column &#40;Mono Q&#8482; GE Healthcare&#41; coupled to a HPLC &#40;1220 Infinity LC&#44; Agilent Technologies&#41; equilibrated with 50<span class="elsevierStyleHsp" style=""></span>mM phosphate buffer&#44; pH 7&#46;4&#46; Retained proteins were eluted with the same buffer containing 1<span class="elsevierStyleHsp" style=""></span>M NaCl&#46; Each fraction was analysed by 16&#37; SDS-PAGE and Coomassie Blue staining to evaluate profilin homogeneity&#46; Protein concentration was determined by the bicinchoninic acid method&#46;</p></span><span id="sec0025" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0055">Immunodetection of profilin</span><p id="par0050" class="elsevierStylePara elsevierViewall"><span class="elsevierStyleItalic">A&#46; palmeri</span> pollen extract and profilin obtained from affinity-chromatography were separated by 16&#37; SDS-PAGE and electro-transferred onto polyvinylidene difluoride &#40;PVDF&#41; membranes &#40;Immobilon-P&#44; Millipore&#41; using standard methods&#46; Membranes were completely dried to block unoccupied sites and prevent nonspecific binding of antibodies&#46; Then&#44; membranes were incubated at room temperature for two hours with a monoclonal antibody against <span class="elsevierStyleItalic">Arabidopsis thaliana</span> profilin &#40;Sigma&#8211;Aldrich<span class="elsevierStyleSup">&#174;</span>&#41; &#40;1&#58;3000 dilution&#41;&#46; After washing with PBS-Tween 0&#46;05&#37;&#44; membranes were incubated for 1<span class="elsevierStyleHsp" style=""></span>h at room temperature with an anti-mouse-IgG-HRP antibody &#40;BioLegend<span class="elsevierStyleSup">&#174;</span>&#41; &#40;1&#58;5000 dilution&#41;&#46; Finally&#44; bound antibodies were detected using 3&#44;3-diaminobenzidine &#40;Sigma&#8211;Aldrich<span class="elsevierStyleSup">&#174;</span>&#41; as substrate&#46;</p></span><span id="sec0030" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0060">Profilin-specific monoclonal antibody binding</span><p id="par0055" class="elsevierStylePara elsevierViewall">The main Mono Q fractions obtained from affinity chromatography fraction were analysed by ELISA&#46; Briefly&#44; immunoplates &#40;Corning Inc&#46;&#41; were coated with 10<span class="elsevierStyleHsp" style=""></span>&#956;g of protein per well diluted in coating buffer &#40;0&#46;05<span class="elsevierStyleHsp" style=""></span>M carbonate bicarbonate buffer pH 9&#46;6&#41;&#46; Plates were incubated overnight at 4<span class="elsevierStyleHsp" style=""></span>&#176;C&#44; washed with PBS-Tween 0&#46;25&#37; and blocked with 5&#37; blocking agent &#40;BLOT-QuickBlocker<span class="elsevierStyleSup">&#174;</span>&#44; Millipore&#41; in PBS at 25<span class="elsevierStyleHsp" style=""></span>&#176;C for 2<span class="elsevierStyleHsp" style=""></span>h&#46; After washing with PBS-Tween solution&#44; 100<span class="elsevierStyleHsp" style=""></span>&#956;l of a monoclonal antibody against <span class="elsevierStyleItalic">A&#46; thaliana</span> profilin &#40;1&#58;5000 dilution&#41; were added in each well and incubated for one hour at room temperature&#46; Plates were washed again and incubated for 1<span class="elsevierStyleHsp" style=""></span>h at room temperature with an anti-mouse-IgG-HRP antibody &#40;1&#58;5000 dilution&#41;&#46; Chromogenic substrate was prepared by adding 50<span class="elsevierStyleHsp" style=""></span>&#956;l of a tetramethylbenzidine &#40;TMB&#41; solution &#40;6<span class="elsevierStyleHsp" style=""></span>mg&#47;ml in dimethyl sulfoxide&#41; and 1&#46;5<span class="elsevierStyleHsp" style=""></span>&#956;l of 3&#37; H<span class="elsevierStyleInf">2</span>O<span class="elsevierStyleInf">2</span> to 2&#46;5<span class="elsevierStyleHsp" style=""></span>ml of 0&#46;1<span class="elsevierStyleHsp" style=""></span>M sodium acetate &#40;pH 5&#46;5&#41; solution&#46; One hundred microlitres of the chromogenic substrate were added to each well&#46; After 15<span class="elsevierStyleHsp" style=""></span>min of incubation in the dark&#44; colour development was stopped by addition of 100<span class="elsevierStyleHsp" style=""></span>&#956;l of 2<span class="elsevierStyleHsp" style=""></span>N H<span class="elsevierStyleInf">2</span>SO<span class="elsevierStyleInf">4</span>&#46; Optical density was read at 450<span class="elsevierStyleHsp" style=""></span>nm using an ELISA plate reader &#40;Stat Fax 303<span class="elsevierStyleSup">&#43;</span>&#44; Awareness Technology&#44; Inc&#46;&#41;&#46;</p></span><span id="sec0035" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0065">Profilin identification by mass spectrometry</span><p id="par0060" class="elsevierStylePara elsevierViewall">Mono Q column fractions that were detected as positive in the ELISA experiment described above&#44; were first analysed by automated Edman degradation on a gas-phase protein sequencer &#40;LF 3000&#44; Beckman Instruments&#44; Irvine&#44; CA&#44; USA&#41;&#46; Because this experiment failed to identify protein &#40;see below&#41;&#44; proteins were then identified by mass spectrometry&#46; For this&#44; other aliquots of Mono Q fractions were submitted to 16&#37; SDS-PAGE and Coomassie blue staining&#46; Bands corresponding to about 14<span class="elsevierStyleHsp" style=""></span>kDa&#44; which is the expected molecular weight for profilin&#44; were manually excised from polyacrylamide gel with a sterile scalpel&#46; Gel pieces were washed twice with 50&#37; &#40;v&#47;v&#41; acetonitrile in 25<span class="elsevierStyleHsp" style=""></span>mM ammonium bicarbonate &#40;pH 8&#46;5&#41; for 15<span class="elsevierStyleHsp" style=""></span>min to remove Coomassie dye&#46; After dehydration with 100&#37; &#40;v&#47;v&#41; acetonitrile for 10<span class="elsevierStyleHsp" style=""></span>min at room temperature&#44; gel pieces were vacuum-dried and rehydrated with sequencing-grade modified trypsin &#40;Promega&#44; Madison&#44; WI&#44; USA&#41; in 25<span class="elsevierStyleHsp" style=""></span>mM ammonium bicarbonate &#40;pH 8&#46;5&#41; at 37<span class="elsevierStyleHsp" style=""></span>&#176;C overnight&#46; Then&#44; in-gel tryptic digested samples were separated by Capillary HPLC and analysed by Electrospray tandem mass spectrometry &#40;ESI-MS&#47;MS&#41; using a 3200 Q TRAP hybrid tandem mass spectrometer &#40;Applied Biosystems&#47;MDS Sciex&#44; Concord&#44; ON&#44; Canada&#41;&#46; Peptide mass and sequence were established from MS data and MS&#47;MS fragmentation patterns of the peptides&#46; Protein identification was performed by searching a non-redundant protein sequence database &#40;NCBI&#41; restricted to green plants using the Mascot search engine &#40;<a id="intr0005" class="elsevierStyleInterRef" href="http://www.matrixscience.com/">http&#58;&#47;&#47;www&#46;matrixscience&#46;com</a>&#41;&#46;</p></span><span id="sec0040" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0070">Detection of IgE against <span class="elsevierStyleItalic">A&#46; palmeri</span> profilin by ELISA</span><p id="par0065" class="elsevierStylePara elsevierViewall">The presence of specific-IgE that recognise <span class="elsevierStyleItalic">A&#46; palmeri</span> profilins was evaluated by ELISA in serum of 15 allergic people with pollinosis&#44; manifested by disease history and positive skin prick test &#40;SPT&#41; to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen extract and other pollens&#46; Five subjects with negative SPT responses were used as negative controls&#46; Briefly&#44; immunoplates were coated with purified profilin as described above&#46; Wells were then incubated with patients&#8217; serum &#40;1&#58;10 in PBS-Tween 0&#46;05&#37;&#41; for 3<span class="elsevierStyleHsp" style=""></span>h at 25<span class="elsevierStyleHsp" style=""></span>&#176;C and 15<span class="elsevierStyleHsp" style=""></span>h at 4<span class="elsevierStyleHsp" style=""></span>&#176;C&#46; After washing&#44; biotinylated anti-human IgE &#40;Zymed<span class="elsevierStyleSup">&#174;</span>&#41; was added to each well &#40;1&#58;4000&#41; and incubated for 2<span class="elsevierStyleHsp" style=""></span>h at 25<span class="elsevierStyleHsp" style=""></span>&#176;C&#46; The immunoplate was washed and incubated for 2<span class="elsevierStyleHsp" style=""></span>h with streptavidin-horseradish peroxidase conjugate &#40;Zymed<span class="elsevierStyleSup">&#174;</span>&#41; at room temperature&#46; Enzymatic reaction was detected using tetramethylbenzidine as substrate&#59; the reaction was stopped with 2<span class="elsevierStyleHsp" style=""></span>N H<span class="elsevierStyleInf">2</span>SO<span class="elsevierStyleInf">4</span> after 15<span class="elsevierStyleHsp" style=""></span>min incubation at room temperature and optical density was read at 450<span class="elsevierStyleHsp" style=""></span>nm &#40;OD<span class="elsevierStyleInf">450</span>&#41;&#46; A sample was considered positive when the OD<span class="elsevierStyleInf">450</span> value was higher than the mean value obtained for SPT negative people plus three standard deviations&#46;</p></span></span><span id="sec0045" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0075">Results</span><span id="sec0050" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0080"><span class="elsevierStyleItalic">A&#46; palmeri</span> pollen has a protein fraction that was recognised by an anti-profilin monoclonal antibody</span><p id="par0070" class="elsevierStylePara elsevierViewall">SDS-PAGE analysis of <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen extract revealed the presence of several proteins with molecular masses ranging from 12 to 75<span class="elsevierStyleHsp" style=""></span>kDa &#40;<a class="elsevierStyleCrossRef" href="#fig0005">Fig&#46; 1</a>A&#41;&#46; Interestingly&#44; profilin-specific monoclonal antibody immunodetected a unique band with a molecular mass of 14<span class="elsevierStyleHsp" style=""></span>kDa&#44; which probably corresponds to <span class="elsevierStyleItalic">A&#46; palmeri</span> profilin &#40;<a class="elsevierStyleCrossRef" href="#fig0005">Fig&#46; 1</a>A&#41;&#46; Because profilins have conserved binding sites for poly-<span class="elsevierStyleSmallCaps">l</span>-proline &#40;pLp&#41;&#44; we purified this allergen from <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen by affinity chromatography using a pLp-Sheparose column&#46; Proteins with pLp affinity were obtained in a single elution fraction &#40;<a class="elsevierStyleCrossRef" href="#fig0005">Fig&#46; 1</a>C&#41; with a yield of 150<span class="elsevierStyleHsp" style=""></span>&#956;g per gram of <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen processed&#46; SDS-PAGE analysis confirmed the presence of a predominant band of about 14<span class="elsevierStyleHsp" style=""></span>kDa&#44; which corresponds to the expected molecular weight for profilin &#40;<a class="elsevierStyleCrossRef" href="#fig0005">Fig&#46; 1</a>B&#41;&#46; Notably&#44; this band was immunodetected by a monoclonal antibody against profilin from <span class="elsevierStyleItalic">A&#46; thaliana</span>&#44; which strongly suggests the presence of homologous proteins in this fraction &#40;<a class="elsevierStyleCrossRef" href="#fig0005">Fig&#46; 1</a>B&#41;&#46;</p><elsevierMultimedia ident="fig0005"></elsevierMultimedia></span><span id="sec0055" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0085"><span class="elsevierStyleItalic">A&#46; palmeri</span> pollen has at least four profilin isoforms</span><p id="par0075" class="elsevierStylePara elsevierViewall">Proteins retained in pLp-Sepharose column were then submitted to anionic-exchange chromatography using a Mono Q column&#46; Results evidenced the separation of seven main fractions &#40;<a class="elsevierStyleCrossRef" href="#fig0010">Fig&#46; 2</a>A&#41;&#46; Notably&#44; fractions F2&#8211;F5 were recognised by a monoclonal antibody against profilin from <span class="elsevierStyleItalic">A&#46; thaliana</span> pollen in ELISA &#40;<a class="elsevierStyleCrossRef" href="#fig0010">Fig&#46; 2</a>B&#41;&#46; Altogether&#44; these results indicate the presence of at least four profilin isoforms in <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen extract&#46;</p><elsevierMultimedia ident="fig0010"></elsevierMultimedia><p id="par0080" class="elsevierStylePara elsevierViewall">Only fractions F4 and F5 were submitted to mass spectrometry analysis&#44; because fractions F2 and F3 were insoluble proteins&#46; In both fractions&#44; mass spectrometry analysis identified two peptides that correspond to the sequence of profilin from other plants&#46; Particularly&#44; peptide 1 &#40;YMVIQGEPGAVIR&#41; totally matches with amino acids 72&#8211;84 in profilin from <span class="elsevierStyleItalic">Hevea brasiliensis</span>&#44; while peptide 2 &#40;LGDYLLDQGL&#41; corresponds to the 122&#8211;131 amino acids region of the same protein&#46; Moreover&#44; regions corresponding to both peptides are highly conserved among allergenic profilins obtained from the allergome database &#40;<a id="intr0010" class="elsevierStyleInterRef" href="http://www.allergome.org/">http&#58;&#47;&#47;www&#46;allergome&#46;org&#47;</a>&#41; and aligned with clustal-W software &#40;<a class="elsevierStyleCrossRef" href="#fig0015">Fig&#46; 3</a>&#41;&#46;</p><elsevierMultimedia ident="fig0015"></elsevierMultimedia></span><span id="sec0060" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0090"><span class="elsevierStyleItalic">A&#46; palmeri</span> profilin is a relevant allergen</span><p id="par0085" class="elsevierStylePara elsevierViewall">Patients&#8217; characteristics and sensitisation profiles are summarised in <a class="elsevierStyleCrossRef" href="#tbl0005">Table 1</a>&#46; Respiratory symptoms of rhinitis were reported in 12 of 15 patients &#40;80&#37;&#41; and rhinitis and asthma symptoms were reported in three of 15 &#40;20&#37;&#41; patients&#46; No food allergy symptoms were reported in any patient&#46; High prevalence of sensitisation to <span class="elsevierStyleItalic">Fraxinus excelsior</span>&#44; <span class="elsevierStyleItalic">Ligustrum vulgare</span>&#44; <span class="elsevierStyleItalic">Chenopodium album</span> and <span class="elsevierStyleItalic">Atriplex stocksii</span> pollen were reported in patients with positive SPT to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen&#46;</p><elsevierMultimedia ident="tbl0005"></elsevierMultimedia><p id="par0090" class="elsevierStylePara elsevierViewall">In order to evaluate the allergenicity of <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen profilin&#44; we analysed serum from 15 individual patients&#8217; with positive SPT to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen extract by ELISA&#44; using the profilins contained in the fraction obtained from affinity chromatography as antigen&#46; Result showed that 9 out of 15 sera contain specific IgE antibodies that recognised profilins coated in wells&#44; representing 60&#37; of the sera tested &#40;<a class="elsevierStyleCrossRef" href="#fig0020">Fig&#46; 4</a>&#41;&#46;</p><elsevierMultimedia ident="fig0020"></elsevierMultimedia></span></span><span id="sec0065" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0095">Discussion</span><p id="par0095" class="elsevierStylePara elsevierViewall">Because of the high amino acid sequence identity between profilins from different organisms and consequently their comparable immunogenicity&#44; profilins have been described as pan-allergens of various plant species&#46;<a class="elsevierStyleCrossRef" href="#bib0275"><span class="elsevierStyleSup">15</span></a> In this study&#44; the identification of profilin from <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen and the presence of profilin-specific IgE antibodies in serum of patients is reported&#46; In <span class="elsevierStyleItalic">A&#46; palmeri</span>&#44; at least four profilin isoforms are expressed in pollen&#44; as demonstrated by anion-exchange chromatography and ELISA using a monoclonal antibody against <span class="elsevierStyleItalic">A&#46; thaliana</span> pollen profilin&#46; Similarly&#44; several isoforms have been reported for allergenic profilin from pollen of <span class="elsevierStyleItalic">Ambrosia artemisiifolia</span> &#40;isoforms Amb a 8&#46;01 and Amb a 8&#46;02&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0280"><span class="elsevierStyleSup">16</span></a><span class="elsevierStyleItalic">Amaranthus viridis</span> &#40;Ama v 2&#46;0101 and Ama v 2&#46;0201&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0285"><span class="elsevierStyleSup">17</span></a><span class="elsevierStyleItalic">Phleum pratense</span> &#40;Phl p 12&#46;0101&#44; Phl p 12&#46;0102&#44; Phl p 12&#46;0103&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0290"><span class="elsevierStyleSup">18</span></a><span class="elsevierStyleItalic">Salsola kali</span> &#40;Sal k 4&#46;0101&#44; Sal k 4&#46;0201&#44; Sal k 4&#46;0301&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0295"><span class="elsevierStyleSup">19</span></a> among other pollens&#46; Purification yield of profilin by affinity chromatography was 150<span class="elsevierStyleHsp" style=""></span>&#956;g&#47;g of pollen&#44; slightly higher than previously reported for other pollens using similar purification protocols&#44; such as sunflower&#44; olive and lambsquarters&#44; which showed yields between 30 and 100<span class="elsevierStyleHsp" style=""></span>&#956;g&#47;g of pollen&#46;<a class="elsevierStyleCrossRefs" href="#bib0300"><span class="elsevierStyleSup">20&#8211;23</span></a> Moreover&#44; purity of profilin after anion-exchange chromatography was more than 95&#37; according to SDS-PAGE and colloidal Coomassie Blue staining&#46;</p><p id="par0100" class="elsevierStylePara elsevierViewall">Fractions &#40;F4 and F5&#41; from anion-exchange chromatography containing profilin isoforms were initially subjected to automated Edman sequencing&#59; however assays failed to release a NH<span class="elsevierStyleInf">2</span>-terminal residue from these fractions &#40;data not shown&#41;&#46; These results suggested the presence of a possible post-translational modification of profilin from <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen&#46; NH<span class="elsevierStyleInf">2</span>-terminal blockage typically occurs when the &#945;-amino groups are acylated or when the N-terminal residue is a pyrrolidone carboxylic acid formed by cyclisation of glutamine&#46;<a class="elsevierStyleCrossRef" href="#bib0320"><span class="elsevierStyleSup">24</span></a> Proteins with serine and alanine termini are the most frequently acetylated&#44; plant profilins display a very high degree of amino acid sequence homology in N-terminal segment &#40;residues 1&#8211;15&#41;&#46;<a class="elsevierStyleCrossRefs" href="#bib0315"><span class="elsevierStyleSup">23&#44;25&#44;26</span></a> Importantly&#44; serine 2 is present in all reported sequences of allergenic profilins from pollen&#44; which reinforced the idea that a post-translational modification is present in <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen profilin isoforms&#44; most likely&#44; an acetylation of the N-terminal serine&#46; Allergenic profilins with blocked N-terminal amino acid have also been reported in melon<a class="elsevierStyleCrossRef" href="#bib0330"><span class="elsevierStyleSup">26</span></a> and olive pollen&#46;<a class="elsevierStyleCrossRef" href="#bib0335"><span class="elsevierStyleSup">27</span></a> This N-terminal modification has also been identified in other plant allergens&#44; such as lipid transfer protein from peach<a class="elsevierStyleCrossRef" href="#bib0340"><span class="elsevierStyleSup">28</span></a> and isoflavone reductase from birch pollen&#46;<a class="elsevierStyleCrossRef" href="#bib0345"><span class="elsevierStyleSup">29</span></a> Because it was not possible to obtain the N-terminal sequence of amino acids from isolated profilin isoforms through Edman degradation method&#44; we performed their identification by mass spectrometry&#46; The detection of two peptides that showed highly conserved amino acid sequence found in profilins from allergenic pollen of a large number of plants&#44; confirmed the identification of profilin isoforms in <span class="elsevierStyleItalic">A&#46; palmeri</span>&#46; Identified peptides are contained in a region that has been previously reported as part of a major IgE binding-site in profilins from <span class="elsevierStyleItalic">H&#46; brasiliensis</span>&#44; <span class="elsevierStyleItalic">Betula pendula</span>&#44; and <span class="elsevierStyleItalic">A&#46; thaliana</span>&#46;<a class="elsevierStyleCrossRef" href="#bib0350"><span class="elsevierStyleSup">30</span></a> Preliminary results obtained by our group show that profilin isoforms identified in this work have a molecular mass of 13&#44;950<span class="elsevierStyleHsp" style=""></span>Da for isoform present in F4 and of 13&#44;958<span class="elsevierStyleHsp" style=""></span>Da for profilin in F5&#44; as judged by MALDI-TOF mass spectrometry analysis &#40;data no shown&#41;&#44; which is consistent with the expected molecular mass for these proteins&#46; This result reinforces earlier evidence that identified allergen belongs to profilin family&#46;</p><p id="par0105" class="elsevierStylePara elsevierViewall">On the other hand&#44; ELISA analysis revealed that 60&#37; of serum from patients with positive SPT to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen showed specific IgE to pooled profilin isoforms&#46; Similar sensitisation rates were observed in patients with positive SPT to <span class="elsevierStyleItalic">F&#46; excelsior</span> pollen &#40;53&#37;&#41;&#46; Slightly lower rates of sensitisation were observed in patients with positive SPT to <span class="elsevierStyleItalic">L&#46; vulgare</span> and <span class="elsevierStyleItalic">A&#46; stocksii</span> pollen &#40;47&#37;&#41;&#44; suggesting a possible role of <span class="elsevierStyleItalic">A&#46; plameri</span> profilin in cross-reactivity among these pollens&#46; Interestingly&#44; patients with positive SPT to <span class="elsevierStyleItalic">C&#46; album</span> pollen&#44; a plant of <span class="elsevierStyleItalic">Amaranthaceae&#47;Chenopodiaceae</span> family&#44; only 33&#37; showed IgE to <span class="elsevierStyleItalic">A&#46; palmeri</span> profilin&#46; In contrary to our finding&#44; previous reports showed sensitisation rates of 55&#37; to profilin from <span class="elsevierStyleItalic">C&#46; album</span> pollen in Spanish patients&#46;<a class="elsevierStyleCrossRef" href="#bib0315"><span class="elsevierStyleSup">23</span></a> It is to note that profilin has been found to be a minor but important allergen in pollen from birch &#40;20&#37;&#41;&#44; timothy &#40;20&#37;&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0275"><span class="elsevierStyleSup">15</span></a> mugwort &#40;20&#8211;36&#37;&#41;&#44;<a class="elsevierStyleCrossRefs" href="#bib0275"><span class="elsevierStyleSup">15&#44;31</span></a> olive &#40;24&#8211;47&#37;&#41;<a class="elsevierStyleCrossRefs" href="#bib0335"><span class="elsevierStyleSup">27&#44;32</span></a> and sunflower &#40;30&#37;&#41;&#46;<a class="elsevierStyleCrossRef" href="#bib0365"><span class="elsevierStyleSup">33</span></a> Nonetheless&#44; it has been found to be a major allergen in other pollens&#44; such as annual mercury &#40;51&#37;&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0370"><span class="elsevierStyleSup">34</span></a> saffron &#40;53&#37;&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0375"><span class="elsevierStyleSup">35</span></a> lambsquarters &#40;55&#37;&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0315"><span class="elsevierStyleSup">23</span></a> date palm &#40;56&#8211;64&#37;&#41;&#44;<a class="elsevierStyleCrossRef" href="#bib0380"><span class="elsevierStyleSup">36</span></a> and soybean &#40;69&#37;&#41;&#46;<a class="elsevierStyleCrossRef" href="#bib0385"><span class="elsevierStyleSup">37</span></a> Similar observations have been reported for profilin of some plant food extract such as muskmelon &#40;71&#8211;100&#37;&#41;&#44;<a class="elsevierStyleCrossRefs" href="#bib0330"><span class="elsevierStyleSup">26&#44;38</span></a> orange &#40;78&#8211;87&#37;&#41;<a class="elsevierStyleCrossRef" href="#bib0395"><span class="elsevierStyleSup">39</span></a> or watermelon&#44; with a rate of profilin-sensitised patients of 56&#37;&#46;<a class="elsevierStyleCrossRef" href="#bib0400"><span class="elsevierStyleSup">40</span></a></p><p id="par0110" class="elsevierStylePara elsevierViewall">In conclusion&#44; we have demonstrated that profilin from <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen is an important allergen for Mexican allergic subjects&#44; which suggests that it can be considered as a panallergen allergen in this allergenic source&#46; Further studies are required to determine whether profilin isoforms represent interesting candidates to be included in desensitisation protocols for people allergic to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen&#46;</p></span><span id="sec0070" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0100">Conflict of interest</span><p id="par0115" class="elsevierStylePara elsevierViewall">The authors have no conflict of interest to declare&#46;</p></span><span id="sec0075" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0105">Ethical disclosures</span><span id="sec0080" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0110">Confidentiality of data</span><p id="par0120" class="elsevierStylePara elsevierViewall">The authors declare that they have followed the protocols of their work centre on the publication of patient data and that all the patients included in the study have received sufficient information and have given their informed consent in writing to participate in that study&#46;</p></span><span id="sec0085" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0115">Right to privacy and informed consent</span><p id="par0125" class="elsevierStylePara elsevierViewall">The authors have obtained the informed consent of the patients and&#47;or subjects mentioned in the article&#46; The author for correspondence is in possession of this document&#46;</p></span><span id="sec0090" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0120">Protection of human subjects and animals in research</span><p id="par0130" class="elsevierStylePara elsevierViewall">The authors declare that the procedures followed were in accordance with the regulations of the responsible Clinical Research Ethics Committee and in accordance with those of the World Medical Association and the Helsinki Declaration&#46;</p></span></span></span>"
    "textoCompletoSecciones" => array:1 [
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        0 => array:3 [
          "identificador" => "xres612835"
          "titulo" => "Abstract"
          "secciones" => array:4 [
            0 => array:2 [
              "identificador" => "abst0005"
              "titulo" => "Background"
            ]
            1 => array:2 [
              "identificador" => "abst0010"
              "titulo" => "Methods"
            ]
            2 => array:2 [
              "identificador" => "abst0015"
              "titulo" => "Principal findings"
            ]
            3 => array:2 [
              "identificador" => "abst0020"
              "titulo" => "Conclusion"
            ]
          ]
        ]
        1 => array:2 [
          "identificador" => "xpalclavsec626628"
          "titulo" => "Keywords"
        ]
        2 => array:2 [
          "identificador" => "sec0005"
          "titulo" => "Introduction"
        ]
        3 => array:3 [
          "identificador" => "sec0010"
          "titulo" => "Materials and methods"
          "secciones" => array:6 [
            0 => array:2 [
              "identificador" => "sec0015"
              "titulo" => "Pollen extract preparation"
            ]
            1 => array:2 [
              "identificador" => "sec0020"
              "titulo" => "Chromatographic isolation of profilin isoforms"
            ]
            2 => array:2 [
              "identificador" => "sec0025"
              "titulo" => "Immunodetection of profilin"
            ]
            3 => array:2 [
              "identificador" => "sec0030"
              "titulo" => "Profilin-specific monoclonal antibody binding"
            ]
            4 => array:2 [
              "identificador" => "sec0035"
              "titulo" => "Profilin identification by mass spectrometry"
            ]
            5 => array:2 [
              "identificador" => "sec0040"
              "titulo" => "Detection of IgE against A&#46; palmeri profilin by ELISA"
            ]
          ]
        ]
        4 => array:3 [
          "identificador" => "sec0045"
          "titulo" => "Results"
          "secciones" => array:3 [
            0 => array:2 [
              "identificador" => "sec0050"
              "titulo" => "A&#46; palmeri pollen has a protein fraction that was recognised by an anti-profilin monoclonal antibody"
            ]
            1 => array:2 [
              "identificador" => "sec0055"
              "titulo" => "A&#46; palmeri pollen has at least four profilin isoforms"
            ]
            2 => array:2 [
              "identificador" => "sec0060"
              "titulo" => "A&#46; palmeri profilin is a relevant allergen"
            ]
          ]
        ]
        5 => array:2 [
          "identificador" => "sec0065"
          "titulo" => "Discussion"
        ]
        6 => array:2 [
          "identificador" => "sec0070"
          "titulo" => "Conflict of interest"
        ]
        7 => array:3 [
          "identificador" => "sec0075"
          "titulo" => "Ethical disclosures"
          "secciones" => array:3 [
            0 => array:2 [
              "identificador" => "sec0080"
              "titulo" => "Confidentiality of data"
            ]
            1 => array:2 [
              "identificador" => "sec0085"
              "titulo" => "Right to privacy and informed consent"
            ]
            2 => array:2 [
              "identificador" => "sec0090"
              "titulo" => "Protection of human subjects and animals in research"
            ]
          ]
        ]
        8 => array:2 [
          "identificador" => "xack206569"
          "titulo" => "Acknowledgments"
        ]
        9 => array:1 [
          "titulo" => "References"
        ]
      ]
    ]
    "pdfFichero" => "main.pdf"
    "tienePdf" => true
    "fechaRecibido" => "2015-02-17"
    "fechaAceptado" => "2015-05-07"
    "PalabrasClave" => array:1 [
      "en" => array:1 [
        0 => array:4 [
          "clase" => "keyword"
          "titulo" => "Keywords"
          "identificador" => "xpalclavsec626628"
          "palabras" => array:4 [
            0 => "Allergen"
            1 => "<span class="elsevierStyleItalic">Amaranthus palmeri</span>"
            2 => "Pollen"
            3 => "Profilin"
          ]
        ]
      ]
    ]
    "tieneResumen" => true
    "resumen" => array:1 [
      "en" => array:3 [
        "titulo" => "Abstract"
        "resumen" => "<span id="abst0005" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0010">Background</span><p id="spar0005" class="elsevierStyleSimplePara elsevierViewall">Pollens represent a rich source of proteins that are also potential elicitors of IgE-mediated pollen allergy&#46; Sensitisation to panallergens could play an important role in diagnosis and specific immunotherapy&#44; because these molecules are present in different plant pollens and plant foods and have marked structural similarity in different species&#46; Profilins are one of the most common panallergens to be studied because they are responsible for a large number of sensitisations and are clearly related to cross-reactivity and co-sensitisation&#46; This study aimed to isolate and characterise a new allergen of <span class="elsevierStyleItalic">Amaranthus palmeri</span> pollen and to determine its allergenicity&#46;</p></span> <span id="abst0010" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0015">Methods</span><p id="spar0010" class="elsevierStyleSimplePara elsevierViewall"><span class="elsevierStyleItalic">A&#46; palmeri</span> pollen profilin was purified using poly-<span class="elsevierStyleSmallCaps">l</span>-proline-Sepharose affinity chromatography followed by anion exchanger chromatography&#46; Identification of purified protein was carried out by mass spectrometry&#46; Specific IgE was estimated in sera of patients with positive skin prick test to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen extract&#44; by enzyme-linked immunosorbent assay &#40;ELISA&#41;&#46;</p></span> <span id="abst0015" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0020">Principal findings</span><p id="spar0015" class="elsevierStyleSimplePara elsevierViewall">Purified protein appeared as a single band at 14<span class="elsevierStyleHsp" style=""></span>kDa in SDS-PAGE gel&#46; Mass spectrometric analysis of the gel band identified two highly conserved peptides corresponding to allergenic profilins from pollen of other plants&#46; Sera from about 60&#37; of allergic patients have IgE that recognises the purified <span class="elsevierStyleItalic">A&#46; palmeri</span> protein&#46;</p></span> <span id="abst0020" class="elsevierStyleSection elsevierViewall"><span class="elsevierStyleSectionTitle" id="sect0025">Conclusion</span><p id="spar0020" class="elsevierStyleSimplePara elsevierViewall">A 14<span class="elsevierStyleHsp" style=""></span>kDa protein of <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen was purified and identified as allergenic profilin&#44; which was recognised by sera from pollen allergic patients&#46;</p></span>"
        "secciones" => array:4 [
          0 => array:2 [
            "identificador" => "abst0005"
            "titulo" => "Background"
          ]
          1 => array:2 [
            "identificador" => "abst0010"
            "titulo" => "Methods"
          ]
          2 => array:2 [
            "identificador" => "abst0015"
            "titulo" => "Principal findings"
          ]
          3 => array:2 [
            "identificador" => "abst0020"
            "titulo" => "Conclusion"
          ]
        ]
      ]
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        "etiqueta" => "Figure 1"
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          "en" => "<p id="spar0025" class="elsevierStyleSimplePara elsevierViewall">Purification of profilin of <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen by Affinity chromatography&#46; &#40;A&#41; SDS-PAGE of pollen extracts&#46; Total and purified proteins were separated on 15&#37; acrylamide gel and stained by colloidal Coomassie blue&#46; Lane 1&#44; molecular weight markers &#40;kDa&#41;&#59; lane 2&#44; total protein extract&#59; lane 3&#44; purified proteins&#46; &#40;B&#41; Immunodetection of profilin&#46; Total and purified proteins were immunodetected by monoclonal antibody against profilin from <span class="elsevierStyleItalic">A&#46; thaliana</span>&#46; Lane 1&#44; total protein extract&#59; lane 2&#44; purified proteins&#46; &#40;C&#41; Elution profile of retained proteins from p-L-p-Sheparose column &#40;arrow indicate addition of 4<span class="elsevierStyleHsp" style=""></span>M of guanidine&#8211;HCl&#41;&#46;</p>"
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        "descripcion" => array:1 [
          "en" => "<p id="spar0030" class="elsevierStyleSimplePara elsevierViewall">Anion-exchange chromatography on Mono Q and ELISA assay&#46; &#40;A&#41; Ion-exchange chromatography of profilin retained from affinity column&#46; Solid line represents A<span class="elsevierStyleInf">280</span>&#59; segmented line represents salt gradient up to 1<span class="elsevierStyleHsp" style=""></span>M NaCl&#46; Major fractions are labelled F1&#8211;F7&#46; &#40;B&#41; Fractions recognised by a monoclonal <span class="elsevierStyleItalic">A&#46; thaliana</span> profilin antibody in ELISA&#46; Antibody against <span class="elsevierStyleItalic">A&#46; thaliana</span> profilin binding with no protein in wells was used as negative control &#40;Ctrl&#8722;&#41;&#46;</p>"
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        "descripcion" => array:1 [
          "en" => "<p id="spar0035" class="elsevierStyleSimplePara elsevierViewall">Comparison of identified <span class="elsevierStyleItalic">A&#46; palmeri</span> peptide amino acid sequences with profilins from other allergenic sources&#46; &#40;A&#41; Peptide 1 &#40;internal peptide&#41; and &#40;B&#41; peptide 2 &#40;C-terminal peptide&#41;&#46; Sequence identity &#40;&#42;&#41; and amino acid changes with conserved physicochemical properties &#40;&#58;&#41; of peptides identified in <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen profilin were identified through compared with sequences of profilins from highly allergenic sources from <span class="elsevierStyleItalic">H&#46; brasiliensis</span> &#40;CAA75312&#41;&#44; <span class="elsevierStyleItalic">A&#46; retroflexus</span> &#40;ACP43298&#41;&#44; <span class="elsevierStyleItalic">A&#46; viridis</span> &#40;ABW37744&#41;&#44; <span class="elsevierStyleItalic">P&#46; pratense</span> &#40;Y09457&#41; and <span class="elsevierStyleItalic">B&#46; verrucosa</span> &#40;P25816&#41;&#46;</p>"
        ]
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        "tipo" => "MULTIMEDIAFIGURA"
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        "descripcion" => array:1 [
          "en" => "<p id="spar0040" class="elsevierStyleSimplePara elsevierViewall">IgE recognition of profilin by individual sera from patients hypersensitive to <span class="elsevierStyleItalic">A&#46; palmeri</span> pollen&#46; ELISA assay responses for sera of 15 patients&#46; A pool of five non-allergic subject serum was used as controls &#40;Ctrls&#8722;&#41;&#46; A sample was considered positive when the OD<span class="elsevierStyleInf">450</span> value was higher than the mean value obtained for skin prick test negative people plus three standard deviations&#46; The error bars indicate the standard deviation between ELISA replicates&#46;</p>"
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        "identificador" => "tbl0005"
        "etiqueta" => "Table 1"
        "tipo" => "MULTIMEDIATABLA"
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        "mostrarDisplay" => false
        "tabla" => array:2 [
          "leyenda" => "<p id="spar0050" class="elsevierStyleSimplePara elsevierViewall"><span class="elsevierStyleItalic">Abbreviations</span>&#58; SPT &#40;&#43;&#41;&#44; positive skin prick test&#46;</p>"
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            0 => array:2 [
              "tabla" => array:1 [
                0 => """
                  <table border="0" frame="\n
                  \t\t\t\t\tvoid\n
                  \t\t\t\t" class=""><thead title="thead"><tr title="table-row"><th class="td" title="table-head  " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Allergen source&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</th><th class="td" title="table-head  " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Rhinitis &#40;<span class="elsevierStyleItalic">n</span>&#47;&#37;&#41;&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</th><th class="td" title="table-head  " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Rhinitis and asthma &#40;<span class="elsevierStyleItalic">n</span>&#47;&#37;&#41;&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</th><th class="td" title="table-head  " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">SPT &#40;&#43;&#41; &#40;<span class="elsevierStyleItalic">n</span>&#47;&#37;&#41;&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</th><th class="td" title="table-head  " align="left" valign="top" scope="col" style="border-bottom: 2px solid black">Specific IgE to <span class="elsevierStyleItalic">A&#46; palmeri</span> profilin &#40;<span class="elsevierStyleItalic">n</span>&#47;&#37;&#41;&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</th></tr></thead><tbody title="tbody"><tr title="table-row"><td class="td" title="table-entry  " align="left" valign="top"><span class="elsevierStyleItalic">Amaranthus palmeri</span>&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">12&#47;80&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">3&#47;20&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">15&#47;100&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">9&#47;60&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry  " align="left" valign="top"><span class="elsevierStyleItalic">Fraxinus excelsior</span>&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">11&#47;73&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">2&#47;13&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">12&#47;80&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">8&#47;53&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry  " align="left" valign="top"><span class="elsevierStyleItalic">Ligustrum vulgare</span>&nbsp;\t\t\t\t\t\t\n
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                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">3&#47;20&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">13&#47;87&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">7&#47;47&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry  " align="left" valign="top"><span class="elsevierStyleItalic">Chenopodium album</span>&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">6&#47;40&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">3&#47;20&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">8&#47;53&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">5&#47;33&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td></tr><tr title="table-row"><td class="td" title="table-entry  " align="left" valign="top"><span class="elsevierStyleItalic">Atriplex stocksii</span>&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">7&#47;47&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">2&#47;13&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">9&#47;60&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td><td class="td" title="table-entry  " align="left" valign="top">7&#47;47&nbsp;\t\t\t\t\t\t\n
                  \t\t\t\t</td></tr></tbody></table>
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Article information

ISSN: 03010546
Original language: English

DOI:10.1016/j.aller.2015.05.002

The statistics are updated each day

Year/Month	Html	Pdf	Total

2024 November	7	1	8
2024 October	23	8	31
2024 September	44	12	56
2024 August	29	8	37
2024 July	16	6	22
2024 June	13	6	19
2024 May	24	7	31
2024 April	31	16	47
2024 March	50	15	65
2024 February	28	7	35
2024 January	37	5	42
2023 December	37	6	43
2023 November	48	5	53
2023 October	60	11	71
2023 September	49	3	52
2023 August	32	13	45
2023 July	45	6	51
2023 June	48	6	54
2023 May	27	9	36
2023 April	25	2	27
2023 March	39	11	50
2023 February	27	13	40
2023 January	23	15	38
2022 December	36	14	50
2022 November	36	11	47
2022 October	30	15	45
2022 September	25	11	36
2022 August	38	11	49
2022 July	25	14	39
2022 June	31	9	40
2022 May	49	6	55
2022 April	73	14	87
2022 March	126	7	133
2022 February	119	10	129
2022 January	100	8	108
2021 December	52	16	68
2021 November	52	11	63
2021 October	49	12	61
2021 September	18	13	31
2021 August	19	5	24
2021 July	57	15	72
2021 June	33	12	45
2021 May	27	7	34
2021 April	59	34	93
2021 March	29	14	43
2021 February	12	9	21
2021 January	18	17	35
2020 December	0	5	5
2020 November	0	1	1
2020 October	0	2	2
2020 September	0	1	1
2020 August	0	2	2
2020 July	0	1	1
2020 May	0	5	5
2020 April	0	5	5
2020 March	0	5	5
2020 February	0	7	7
2020 January	0	6	6
2019 December	0	1	1
2019 October	0	2	2
2019 September	0	1	1
2019 August	0	11	11
2019 July	0	10	10
2019 June	0	16	16
2019 May	0	33	33
2019 April	0	13	13
2019 March	0	3	3
2019 February	0	3	3
2019 January	0	4	4
2018 December	0	2	2
2018 August	0	6	6
2018 July	0	2	2
2018 February	6	7	13
2018 January	9	2	11
2017 December	1	3	4
2017 November	11	12	23
2017 October	8	6	14
2017 September	7	4	11
2017 August	9	3	12
2017 July	5	6	11
2017 June	4	4	8
2017 May	10	6	16
2017 April	7	6	13
2017 March	7	53	60
2017 February	9	14	23
2017 January	6	1	7
2016 December	0	4	4
2016 October	0	6	6
2016 September	0	8	8
2016 August	0	1	1
2016 June	0	2	2
2016 March	3	2	5

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Allergologia et Immunopathologia is no longer published on Elsevier since the 2021 year.Transferred to Codon Publications

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Allergologia et Immunopathologia is no longer published on Elsevier since the 2021 year.Transferred to Codon Publications

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