Skip to content

Structural and Functional Analysis of Cell Wall-Anchored PolypeptideAdhesin BspA in Streptococcus agalactiae

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)15985-16000
Number of pages16
JournalJournal of Biological Chemistry
Volume291
Issue number31
Early online date15 Jun 2016
DOIs
DateAccepted/In press - 15 Jun 2016
DateE-pub ahead of print - 15 Jun 2016
DatePublished (current) - 29 Jul 2016

Abstract

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 immune-compromised 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 β-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.

    Research areas

  • adhesin, AgI/II polypeptide, Streptococcus, virulence factor, Candida albicans, crystallography, circular dichroism (CD), isothermal titration calorimetry (ITC), molecular dynamics

Download statistics

No data available

Documents

Documents

  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via ASBMB at http://www.jbc.org/content/early/2016/06/15/jbc.M116.726562.abstract. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 1 MB, PDF document

DOI

View research connections

Related faculties, schools or groups