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Lookup NU author(s): Professor Paul RaceORCiD
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© 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Streptococcus agalactiae (group B Streptococcus, GBS) is the predominant cause of early-onset infectious disease in neonates and is responsible for life-threatening infections in elderly and immunocompromised individuals. Clinical manifestations of GBS infection include sepsis, pneumonia, and meningitis. Here, we describe BspA, a deviant antigen I/II family polypeptide that confers adhesive properties linked to pathogenesis in GBS. Heterologous expression of BspA on the surface of the non-adherent bacterium Lactococcus lactis confers adherence to scavenger receptor gp340, human vaginal epithelium, and to the fungus Candida albicans. Complementary crystallographic and biophysical characterization of BspA reveal a novel →-sandwich adhesion domain and unique asparagine-dependent super-helical stalk. Collectively, these findings establish a new bacterial adhesin structure that has in effect been hijacked by a pathogenic Streptococcus species to provide competitive advantage in human mucosal infections.
Author(s): Rego S, Heal TJ, Pidwill GR, Till M, Robson A, Lamont RJ, Sessions RB, Jenkinson HF, Race PR, Nobbs AH
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2016
Volume: 291
Issue: 31
Pages: 15985-16000
Print publication date: 29/07/2016
Online publication date: 15/06/2016
Acceptance date: 02/04/2016
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology Inc.
URL: https://doi.org/10.1074/jbc.M116.726562
DOI: 10.1074/jbc.M116.726562
PubMed id: 27311712
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