Article information
Resumen
Las ficolinas son proteínas de defensa que forman oligómeros a partir de tallos homólogos al colágeno y dominios semejantes a fibrinógeno. Son capaces de sentir señales de peligro tales como patrones moleculares asociados patógenos o a células apoptóticas. En el hombre, las ficolinas L y H se han caracterizado en el suero, mientras que la ficolina M es secretada por células monocíticas. Al igual que la lectina de unión a manano (“mannan-binding lectin”, MBL), pueden asociarse a las serina-proteasas asociadas a MBL e iniciar la vía de activación de complemento de las lectinas, un importante sistema efector de la inmunidad innata humoral. También pueden actuar como opsoninas, incrementando la eliminación de sus dianas por fagocitosis. Estudios estructurales recientes muestran que la ficolina L es una proteína de reconocimiento versátil, capaz de unir moléculas acetiladas y carbohidratos neutros por medio de sitios de unión diferentes, mientras que la ficolina H posee un único sitio de unión con una especificidad más restringida hacia los carbohidratos neutros. Los estudios filogenéticos revelan que las ficolinas han sido conservadas en el proceso evolutivo, apoyando la hipótesis de que el sistema de complemento primitivo era un sistema de opsonización basado en lectinas, y ponen de relieve la importancia de las proteínas de reconocimiento de carbohidratos en la inmunidad innata.
Palabras clave:
Ficolina
Inmunidad Innata
Receptores de reconocimiento de modelos
Activación del Complemento
MASP
Abstract
Ficolins are oligomeric defence proteins assembled from collagen-like stalks and fibrinogen-like domains that are able to sense danger signals such as pathogen- or apoptotic cell-associated molecular patterns. In humans, L- and H-ficolins have been characterized in serum whereas M-ficolin is secreted by monocytic cells. Like mannan-binding lectin (MBL), they are able to associate with MBL-associated serine proteases and to trigger activation of the lectin pathway of complement, a major effector system of humoral innate immunity. They can also act as opsonins to enhance clearance of their targets by phagocytosis. Recent structural studies have shown that L-ficolin is a versatile recognition protein able to bind acetylated molecules and neutral carbohydrates through different binding sites, whereas H-ficolin has a single binding site with a more restricted specificity for neutral carbohydrates. Phylogenetic studies reveal that ficolins have been conserved through evolution, supporting the hypothesis that the primitive complement system was a lectin-based opsonic system, and emphasizing the essential role of carbohydrate recognition proteins in innate immunity.
Key words:
Ficolin
Innate immunity
Pattern recognition receptor
Complement activation
MASP
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