TY - JOUR
T1 - Cooperative binding of two antibodies to independent antigens by an Fc-dependent mechanism
AU - Greenspan, N. S.
AU - Dacek, D. A.
AU - Cooper, L. J.N.
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1989
Y1 - 1989
N2 - 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 Glc-NAc-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.
AB - 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 Glc-NAc-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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U2 - 10.1096/fasebj.3.10.2666233
DO - 10.1096/fasebj.3.10.2666233
M3 - Article
C2 - 2666233
AN - SCOPUS:0024395005
SN - 0892-6638
VL - 3
SP - 2203
EP - 2207
JO - FASEB Journal
JF - FASEB Journal
IS - 10
ER -