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.

journal_name

Immunobiology

journal_title

Immunobiology

authors

Hunold K,Weber-Steffens D,Runza VL,Jensenius JC,Männel DN

doi

10.1016/j.imbio.2012.01.013

subject

Has Abstract

pub_date

2012-10-01 00:00:00

pages

982-5

issue

10

eissn

0171-2985

issn

1878-3279

pii

S0171-2985(12)00017-4

journal_volume

217

pub_type

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