Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1

Show simple item record Ramsland, P en Willoughby, NL en Trist, H en Farrugia, W en Hogarth, PM en Fraser, John en Wines, B en 2012-05-23T00:38:41Z en 2007 en
dc.identifier.citation PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 104(38):15051-15056 18 Sep 2007 en
dc.identifier.issn 0027-8424 en
dc.identifier.uri en
dc.description.abstract Infection by Staphylococcus aureus can result in severe conditions such as septicemia, toxic shock, pneumonia, and endocarditis with antibiotic resistance and persistent nasal carriage in normal individuals being key drivers of the medical impact of this virulent pathogen. In both virulent infection and nasal colonization, S. aureus encounters the host immune system and produces a wide array of factors that frustrate host immunity. One in particular, the prototypical staphylococcal superantigen-like protein SSL7, potently binds IgA and C5, thereby inhibiting immune responses dependent on these major immune mediators. We report here the three-dimensional structure of the complex of SSL7 with Fc of human IgA1 at 3.2 Å resolution. Two SSL7 molecules interact with the Fc (one per heavy chain) primarily at the junction between the Cα2 and Cα3 domains. The binding site on each IgA chain is extensive, with SSL7 shielding most of the lateral surface of the Cα3 domain. However, the SSL7 molecules are positioned such that they should allow binding to secretory IgA. The key IgA residues interacting with SSL7 are also bound by the leukocyte IgA receptor, FcαRI (CD89), thereby explaining how SSL7 potently inhibits IgA-dependent cellular effector functions mediated by FcαRI, such as phagocytosis, degranulation, and respiratory burst. Thus, the ability of S. aureus to subvert IgA-mediated immunity is likely to facilitate survival in mucosal environments such as the nasal passage and may contribute to systemic infections. en
dc.publisher National Academy of Sciences en
dc.relation.ispartofseries Proceedings of the National Academy of Sciences of the United States of America en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from en
dc.rights.uri en
dc.title Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1 en
dc.type Journal Article en
dc.identifier.doi 10.1073/pnas.0706028104 en
pubs.issue 38 en
pubs.begin-page 15051 en
pubs.volume 104 en
dc.rights.holder Copyright: National Academy of Sciences en
dc.identifier.pmid 17848512 en
pubs.end-page 15056 en
dc.rights.accessrights en
pubs.subtype Article en
pubs.elements-id 74191 en Medical and Health Sciences en Science en Science Research en Maurice Wilkins Centre (2010-2014) en
pubs.record-created-at-source-date 2010-09-01 en
pubs.dimensions-id 17848512 en

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