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Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae

DOI: 10.1074/jbc.M116.726562 DOI Help

Authors: Sara Rego (School of Oral and Dental Sciences, University of Bristol; School of Biochemistry, University of Bristol) , Timothy J. Heal (School of Biochemistry, University of Bristol; Bristol Centre for Functional Nanomaterials, University of Bristol) , Grace R. Pidwill (School of Oral and Dental Sciences, University of Bristol) , Marisa Till (School of Biochemistry, University of Bristol) , Alice Robson (School of Biochemistry, University of Bristol) , Richard J. Lamont (Department of Oral Immunology and Infectious Diseases, University of Louisville) , Richard B. Sessions (School of Biochemistry, University of Bristol) , Howard F. Jenkinson (School of Oral and Dental Sciences, University of Bristol) , Paul R. Race (School of Biochemistry, University of Bristol) , Angela H. Nobbs (School of Oral and Dental Sciences, University of Bristol)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 291 , PAGES 15985 - 16000

State: Published (Approved)
Published: July 2016
Diamond Proposal Number(s): 8922

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 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 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.

Journal Keywords: adhesin; bacterial adhesion; bacterial pathogenesis; Candida albicans; protein conformation; Streptococcus; structural model; structure-function; x-ray crystallography; AgI/II family polypeptide

Subject Areas: Biology and Bio-materials, Medicine, Chemistry


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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