Year: 2013
Type: article
Abstract: Background: Collectins and ficolins are important in the clearance of endogenous and exogenous danger materials.A new human collectin-11 was recently identified in serum with low concentration in complex with mannose-binding lectin (MBL)/ficolin-associated serine proteases, and found to recognize carbohydrate residues present on various microorganisms.Objectives: We hypothesized that collectin-11 could be a novel initiation molecule in the lectin complement pathway in addition to the MBL and the ficolins.Methods: The association of MASP-1, -2, -3 and MAP-1 with collectin-11 was analyzed by the ELISA platform and by flow cytometry using Candida albicans as collectin-11 binding matrix.The potential involvement of collectin-11 in activation of the lectin complement pathway was evaluated by addition of exogenous recombinant MASP-2 and purified human C4 to collectin-11 anchored on Candida albicans using flow cytometry.Moreover, we investigated the depositions of C4, C3 and the terminal complement complex (TCC) in the presence of collectin-11 on Candida albicans by using MBL-defect serum as complement source.Results: We found that collectin-11 could associate with all the known MASPs (MASP-1, -2, -3) as well as the lectin pathway regulator MAP-1, and revealed that collectin-11:MASP-2 complex formation on Candida albicans could mediate C4 deposition.Furthermore, collectin-11 anchored on Candida albicans induced depositions of C4, C3 and formation of TCC in the presence of MBL-defect serum.Conclusions: These results define collectin-11 as the fifth recognition molecule in the lectin complement pathway in addition to MBL, ficolin-1, ficolin-2 and ficolin-3.
DOI: 10.1111/sji.12036
Institutions: Physiologie, Environnement et Génétique pour l'Animal et les Systèmes d'Elevage, Lifepharms (United States), Novo Nordisk (Denmark), Génétique Animale et Biologie Intégrative, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Infectiologie et santé publique, Cobb-Vantress (United States)
Language: English
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W4297440955
