5DZA

Streptococcus agalactiae AgI/II polypeptide BspA C terminal domain (WT)

Summary for 5DZA

• Entry DOI: 10.2210/pdb5dza/pdb
• Descriptor: BspA, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: adhesin, cell adhesion
• Biological source: Streptococcus agalactiae serotype III (strain NEM316)
• Total number of polymer chains: 1
• Total formula weight: 36722.43

Authors

Rego, S.,Till, M.,Race, P.R. (deposition date: 2015-09-25, release date: 2016-06-22, Last modification date: 2024-11-20)

Primary citation

Rego, S.,Heal, T.J.,Pidwill, G.R.,Till, M.,Robson, A.,Lamont, R.J.,Sessions, R.B.,Jenkinson, H.F.,Race, P.R.,Nobbs, A.H.
Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae.
J.Biol.Chem., 291:15985-16000, 2016

PubMed 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.

PubMed: 27311712
DOI: 10.1074/jbc.M116.726562

Experimental method

X-RAY DIFFRACTION (2.19 Å)