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M‐ficolin, an Innate Immune Defence Molecule, Binds Patterns of Acetyl Groups and Activates Complement
Author(s) -
Frederiksen P. D.,
Thiel S.,
Larsen C. B.,
Jensenius J. C.
Publication year - 2005
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.2005.01685.x
Subject(s) - ficolin , lectin pathway , complement system , innate immune system , proteases , collectin , biology , lectin , recombinant dna , mannan binding lectin , biochemistry , serine , anaphylatoxin , classical complement pathway , immune system , chemistry , immunology , receptor , enzyme , gene
Ficolins play a role in the innate immune defence as pathogen‐associated molecular pattern recognition molecules. Three ficolins are found in humans: H‐ficolin, L‐ficolin and M‐ficolin. L‐ficolin and H‐ficolin circulate in blood in complexes with mannan‐binding lectin‐associated serine proteases (MASPs) and are capable of activating the complement system. L‐ficolin shows affinity for acetylated compounds and binds to various capsulated strains of bacteria. H‐ficolin has been shown to bind Aerococcus viridans . Less is known about M‐ficolin, but it is thought to be present only on monocytes. We have synthesized recombinant M‐ficolin and find that it, in a manner similar to L‐ficolin, is able to bind to acetylated compounds and to associate with recombinant MASP‐2. Upon binding to M‐ficolin ligands, the associated MASP‐2 zymogen is activated and cleaves C4, thus triggering the complement system. We developed a monoclonal rat anti‐human‐M/L‐ficolin antibody and verified by flow cytometric analysis the presence of ficolin on the surface of peripheral blood monocytes.