Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded beta-helix.

@article{Smith2005StructureOA,
  title={Structure of a group A streptococcal phage-encoded virulence factor reveals a catalytically active triple-stranded beta-helix.},
  author={Nicola L. Smith and Edward J Taylor and Anna-Marie Lindsay and S. Charnock and Johan P. Turkenburg and Eleanor J. Dodson and Gideon J. Davies and Gary W Black},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 49},
  pages={
          17652-7
        }
}
  • N. Smith, E. Taylor, +5 authors G. Black
  • Published 2005
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
Streptococcus pyogenes (group A Streptococcus) causes severe invasive infections including scarlet fever, pharyngitis (streptococcal sore throat), skin infections, necrotizing fasciitis (flesh-eating disease), septicemia, erysipelas, cellulitis, acute rheumatic fever, and toxic shock. The conversion from nonpathogenic to toxigenic strains of S. pyogenes is frequently mediated by bacteriophage infection. One of the key bacteriophage-encoded virulence factors is a putative "hyaluronidase," HylP1… Expand
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