Structure of the C‐terminal domain of AspA (antigen I/II‐family) protein from Streptococcus pyogenes. Issue 1 (12th March 2014)

• Record Type: Journal Article
• Authors: Hall, Michael; Nylander, Åsa; Jenkinson, Howard F.; Persson, Karina
• Is Part Of: FEBS open bio. Volume 4:Issue 1(2014)
• Page Start: 283
• Page End: 289
• Publication Date: 2014-03-12
• Subjects: Antigen I/II -- Isopeptide bond -- Adhesin -- X-ray crystallography; Molecular biology -- Periodicals; Cytology -- Periodicals; Life sciences -- Periodicals; Biological Science Disciplines -- Periodicals; Molecular Biology -- Periodicals; Cell Biology -- Periodicals; Cytology; Life sciences; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.fob.2014.02.012
• Languages: English
• ISSNs: 2211-5463

Abstract

Abstract : The pathogenic bacteria Streptococcus pyogenes can cause an array of diseases in humans, including moderate infections such as pharyngitis (strep throat) as well as life threatening conditions such as necrotizing fasciitis and puerperal fever. The antigen I/II family proteins are cell wall anchored adhesin proteins found on the surfaces of most oral streptococci and are involved in host colonization and biofilm formation. In the present study we have determined the crystal structure of the C2–3 ‐domain of the antigen I/II type protein AspA from S. pyogenes M type 28. The structure was solved to 1.8 Å resolution and shows that the C2–3 ‐domain is comprised of two structurally similar DEv‐IgG motifs, designated C2 and C3, both containing a stabilizing covalent isopeptide bond. Furthermore a metal binding site is identified, containing a bound calcium ion. Despite relatively low sequence identity, interestingly, the overall structure shares high similarity to the C2–3 ‐domains of antigen I/II proteins from Streptococcus gordonii and Streptococcus mutans, although certain parts of the structure exhibit distinct features. In summary this work constitutes the first step in the full structure determination of the AspA protein from S. pyogenes . Abstract : The structure of the C2–3 ‐domain of AspA from S. pyogenes was determined. The C2 and C3 domains both adopt DEv‐IgG folds. Conserved isopeptide bonds and calcium binding sites are observed. Distinct structural features are observed in the SspB Adherence Region (BAR).