Molecular population genetic analysis of a Streptococcus pyogenes bacteriophage-encoded hyaluronidase gene: recombination contributes to allelic variation

Microb Pathog. 1997 Apr;22(4):209-17. doi: 10.1006/mpat.1996.9999.


Many strains of the human pathogenic bacterium Streptococcus pyogenes produce hyaluronidase, an enzyme that degrades hyaluronic acid, a major component of the extracellular matrix. Degradation of hyaluronic acid is thought to aid in host tissue invasion and dissemination of S. pyogenes. The molecular population genetics of the bacteriophage-encoded hyaluronidase gene (hyl) was analysed by sequencing the gene from 13 streptococcal strains representing seven well-differentiated multilocus enzyme electrophoretic types and eight M or T protein serotypes. Substantial levels of allelic polymorphism were identified, and the analysis found strong statistical evidence that recombinational processes have contributed to the generation of molecular variation in this gene. A 111 base pair segment of hyl encoding a collagenous motif, that may bind collagen, was absent in a serotype M14 isolate and 13 serotype M18 multilocus enzyme electrophoretic type 20 strains examined. The analysis provides a molecular population genetics framework for studies examining the role of naturally occurring hyaluronidase variation in host-pathogen interactions.

Publication types

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

MeSH terms

  • Alleles*
  • Base Sequence
  • Collagen / genetics
  • DNA, Viral
  • Genetic Variation*
  • Humans
  • Hyaluronoglucosaminidase / genetics*
  • Molecular Sequence Data
  • Recombination, Genetic
  • Sequence Analysis, DNA
  • Streptococcus Phages / enzymology*
  • Streptococcus Phages / genetics
  • Streptococcus pyogenes / virology
  • Viral Proteins / genetics*


  • DNA, Viral
  • Viral Proteins
  • Collagen
  • Hyaluronoglucosaminidase