A 28-kilodalton fibronectin-binding protein of group A streptococci

Curr Microbiol. 1992 Nov;25(5):245-50. doi: 10.1007/BF01575856.

Abstract

Lipoteichoic acid (LTA) has been implicated as a major adhesin of group A streptococci that interacts with fibronectin (Fn). It has been suggested that protein adhesins may also be involved in the binding of Fn to streptococci. We searched for such a protein by transblotting membrane preparations from M types 5, 19, and 24 group A streptococci to nitrocellulose and reacting the blot with 125I-Fn. The Fn reacted with a 28-kDa polypeptide from all three serotypes of streptococci. Using affinity-purified antibodies to the 28-kDa protein in immunoblots of membrane preparations from various streptococci, we demonstrated that the 28-kDa protein is present in all 17 strains tested. Affinity-purified antibodies to the 28-kDa protein also reacted in varying degrees with intact streptococci, demonstrating that the antigen is exposed on the surface of intact organisms. Our results suggest that, in addition to LTA, group A streptococci contain a common Fn-binding moiety that is expressed as a major component of membrane preparations and that is accessible on the surface of streptococci for interactions with Fn.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adhesins, Bacterial*
  • Bacterial Outer Membrane Proteins / drug effects
  • Bacterial Outer Membrane Proteins / isolation & purification*
  • Bacterial Proteins*
  • Carrier Proteins*
  • Fibronectins / metabolism*
  • Molecular Weight
  • Protein Binding
  • Serotyping
  • Streptococcus pyogenes / chemistry*
  • Streptococcus pyogenes / classification

Substances

  • Adhesins, Bacterial
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Carrier Proteins
  • Fibronectins
  • fibronectin-binding proteins, bacterial