Identification of a Ficolin-like Serum Lectin of the Common Carp as a Novel Homologue of Mammalian Microfibrillar-Associated Protein 4

Serum lectins in vertebrates play crucial roles in innate immunity as recognition molecules for pathogen-associated molecular patterns (PAMPs). In mammals, two major lectins, mannose-binding lectin (MBL) and ficolin, both containing N-terminal collagen-like domains, activate the lectin pathway of complement. While MBL and ficolin recognize distinct PAMPs, their counterparts in teleosts are less understood. To date, MBL and galactose-binding lectin (GalBL) have been identified in teleosts, but the presence of ficolin remains unclear. In this study, we purified a 31-kDa serum lectin from common carp that displayed carbohydrate-binding specificity similar to that of mammalian ficolin. Unexpectedly, this lectin lacked an N-terminal collagenous domain and showed the highest similarity to mammalian microfibril-associated glycoprotein 4 (MFAP4), suggesting that the lectin is distinct from fibulin. Biochemical analyses revealed that carp MFAP4-like lectin (MFAP4Lec) protein forms a hexamer in serum, specifically binds GlcNAc and GalNAc, and recognizes the fish pathogen Vibrio anguillarum. The binding was competitively inhibited by GlcNAc but not by EDTA, indicating Ca2+-independent recognition. These findings suggest that MFAP4Lec functions as a novel serum lectin in teleost fish, serving as a recognition molecule for bacterial pathogens in innate immunity.