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Publication - Dr Paul Race

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

    Citation

    Rego, S, Heal, TJ, Pidwill, GR, Till, M, Robson, A, Lamont, R, Sessions, RB, Jenkinson, HF, Race, PR & Nobbs, AH, 2016, ‘Structural and Functional Analysis of Cell Wall-Anchored PolypeptideAdhesin BspA in Streptococcus agalactiae’. Journal of Biological Chemistry, vol 291., pp. 15985-16000

    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.

    Full details in the University publications repository