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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
Issue number31
Early online date15 Jun 2016
DateAccepted/In press - 15 Jun 2016
DateE-pub ahead of print - 15 Jun 2016
DatePublished (current) - 29 Jul 2016


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

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