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Structural and functional analysis of cell wall-anchored polypeptide adhesin BspA in Streptococcus agalactiae

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.

Publication metadata

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.


DOI: 10.1074/jbc.M116.726562

PubMed id: 27311712


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