The role of Fc-FcγR interactions in IgG-mediated microbial neutralization.
Antibodies are bifunctional molecules, containing a variable Fab domain that mediates binding specificity and a constant Fc domain that bridges antibody-coated targets with FcγR-expressing cells that mediate effector functions. Although traditional mechanisms of antibody-mediated neutralization of microbes have been largely thought to result from Fab-antigen interactions, recent studies suggest that recruitment of FcγR-expressing effector cells by antibodies is a major in vivo mechanism of antibody-mediated protection from infection. In this article, we review FcγR biology, compare mammalian FcγR families, and summarize recent evidence demonstrating the crucial role that Fc-FcγR interactions play during in vivo protection from infection.
The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065.
Stylianos
S
Bournazos
The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065.
David J
DJ
DiLillo
The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065 ravetch@rockefeller.edu.
Jeffrey V
JV
Ravetch
D000818:Animals; D057134:Antibodies, Neutralizing / Q000276:immunology*; D000937:Antigen-Antibody Reactions; D005786:Gene Expression Regulation / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D007239:Infections / Q000276:immunology* / Q000473:pathology; D017452:Receptors, IgG / Q000276:immunology*
D057134:Antibodies, Neutralizing; D007074:Immunoglobulin G; D017452:Receptors, IgG