Functional analysis of mouse ficolin-B and detection in neutrophils

Abstract Ficolins and mannan-binding lectin recognize pathogen-associated molecular patterns and initiate the lectin pathway of complement activation via the associated serine proteases. In contrast to human ficolins and mouse ficolin-A, mouse ficolin-B has been considered incapable of complement activation. Dose-dependent binding of recombinant ficolin-B to immobilized GlcNAc, acetylated BSA, acetylated LDL, and fetuin was detected with ficolin-B-specific monoclonal antibodies. Recombinant ficolin-B bound to immobilized acetylated bovine serum albumin interacted with recombinant human mannan-binding lectin-associated serine protease-2, which led to C4 cleavage, thus demonstrating the capability of ficolin-B to activate the lectin pathway. Ficolin-B-specific monoclonal antibodies identified natural ficolin-B protein in lysates of mouse granulocytes isolated from the bone marrow. These results identify mouse ficolin-B as a functional member of the ficolin family activating complement via the lectin pathway.