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

Ann Marie Marciel, Vivek Kapur, James M. Musser

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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.

Original languageEnglish (US)
Pages (from-to)209-217
Number of pages9
JournalMicrobial Pathogenesis
Issue number4
StatePublished - Apr 1997


All Science Journal Classification (ASJC) codes

  • Microbiology
  • Infectious Diseases

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