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Jens Christian Jensenius

M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement

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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.
Original languageEnglish
JournalScandinavian Journal of Immunology
Volume62
Issue5
Pages (from-to)462-73
Number of pages12
ISSN0300-9475
DOIs
Publication statusPublished - 2005

    Research areas

  • Acetylation, Animals, Antibodies, Monoclonal, Binding, Competitive, Blotting, Western, Calcium, Cell Line, Complement Activation, Complement C4, Complement C4b, Humans, Immunity, Innate, Lectins, Mannose-Binding Protein-Associated Serine Proteases, Membrane Proteins, Molecular Weight, Monocytes, Protein Binding, Rats, Recombinant Proteins, Serum Albumin

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