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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 m...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4548051/ https://www.ncbi.nlm.nih.gov/pubmed/26282878 http://dx.doi.org/10.1084/jem.20151267 |
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author | Bournazos, Stylianos DiLillo, David J. Ravetch, Jeffrey V. |
author_facet | Bournazos, Stylianos DiLillo, David J. Ravetch, Jeffrey V. |
author_sort | Bournazos, Stylianos |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4548051 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-45480512016-02-24 The role of Fc–FcγR interactions in IgG-mediated microbial neutralization Bournazos, Stylianos DiLillo, David J. Ravetch, Jeffrey V. J Exp Med Review 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 Rockefeller University Press 2015-08-24 /pmc/articles/PMC4548051/ /pubmed/26282878 http://dx.doi.org/10.1084/jem.20151267 Text en © 2015 Bournazos et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Review Bournazos, Stylianos DiLillo, David J. Ravetch, Jeffrey V. The role of Fc–FcγR interactions in IgG-mediated microbial neutralization |
title | The role of Fc–FcγR interactions in IgG-mediated microbial neutralization |
title_full | The role of Fc–FcγR interactions in IgG-mediated microbial neutralization |
title_fullStr | The role of Fc–FcγR interactions in IgG-mediated microbial neutralization |
title_full_unstemmed | The role of Fc–FcγR interactions in IgG-mediated microbial neutralization |
title_short | The role of Fc–FcγR interactions in IgG-mediated microbial neutralization |
title_sort | role of fc–fcγr interactions in igg-mediated microbial neutralization |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4548051/ https://www.ncbi.nlm.nih.gov/pubmed/26282878 http://dx.doi.org/10.1084/jem.20151267 |
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