The FASEB Journal, Vol 3, 2203-2207, Copyright © 1989 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Cooperative binding of two antibodies to independent antigens by an Fc- dependent mechanism

NS Greenspan, DA Dacek and LJ Cooper
Institute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106.

Binding of a murine N-acetylglucosamine (GlcNAc)-specific IgG3 monoclonal antibody to a solid phase expressing GlcNAc determinants and phosphocholine (PC) determinants is enhanced by IgG3, but not IgG2b, PC- specific monoclonal antibody. The cooperative binding requires an intact Fc region on the GlcNAc-specific monoclonal antibody and is hypothesized to result from Fc-Fc association. Although the in vivo relevance of this phenomenon requires further study, intermolecular cooperativity in binding of antibody to multivalent antigens, such as bacterial cell wall antigens, could represent an adaptive mechanism for antibodies expressing low intrinsic affinities for highly repeated epitopes. Furthermore, the ability of antibodies of distinct specificity to participate in cooperative binding offers, at least in principle, new approaches to optimizing antibody targeting.

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