The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase

Microbiology. 1996 Aug;142 ( Pt 8):2311-20. doi: 10.1099/13500872-142-8-2311.

Abstract

Group A streptococci bind the serine protease plasmin with high affinity. Previously, a 41 kDa protein was identified as a candidate plasmin receptor protein (Plr) from group A streptococcal strain 64/14. The plr gene encoding Plr was cloned and the deduced amino acid sequence of Plr had significant similarity to glyceraldehyde-3-phosphate dehydrogenases (GAPDHs). In this study we have isolated cytoplasmic GAPDH of streptococcal strain 64/14. This enzyme was examined, on both structural and functional levels, for its relatedness to the Plr of strain 64/14 purified from mutanolysin extract and to recombinant Plr. We report here that no differences were detected between streptococcal Plr and cytoplasmic GAPDH on the basis of antibody reactivity, plasmin-binding activity, GAPDH activity, N-terminal amino acid sequence, peptide map analysis by V8 protease digestion and amino acid composition analysis. Furthermore, the plr gene appears to be present as a single copy in group A streptococci.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Bacterial Proteins*
  • Chromatography, Affinity
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli
  • Fibrinolysin / metabolism*
  • Genes, Bacterial
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / isolation & purification
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism*
  • Immunoblotting
  • Kinetics
  • Peptide Mapping
  • Receptors, Peptide / chemistry*
  • Receptors, Peptide / isolation & purification
  • Receptors, Peptide / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Restriction Mapping
  • Streptococcus pyogenes / genetics
  • Streptococcus pyogenes / metabolism*

Substances

  • Amino Acids
  • Bacterial Proteins
  • Plr protein, Streptococcus
  • Receptors, Peptide
  • Recombinant Proteins
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Fibrinolysin