The role of Fc-FcγR interactions in IgG-mediated microbial neutralization

Stylianos Bournazos1, David J DiLillo1, Jeffrey V Ravetch2

  • 1The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065.

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.

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