Structural evidence for the evolution of pyrogenic toxin superantigens

David T. Mitchell, David G Levitt, Patrick M. Schlievert, Douglas H Ohlendorf

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

Pathogenic bacteria have evolved a wide variety of toxins to invade and attack host organisms. In particular, strains of the bacteria Staphylococcus aureus and Streptococcus pyogenes produce a family of pyrogenic toxin superantigens (PTSAgs) that can cause illness, e.g., toxic shock syndrome, or synergize with a number of other immune system disorders. The PTSAgs are all similar in size and have a conserved two-domain tertiary fold despite minimal amino acid sequence identity. The tertiary structure of PTSAg domain 1 is similar to the immunoglobulin binding motif of streptococcal proteins G and L. PTSAg domain 2 resembles members of the oligosaccharide/oligonucleotide binding fold family that includes the B subunits of the AB5 heat-labile enterotoxins, cholera toxin, pertussis toxin, and vetotoxin. The strong structural homology between the pyrogenic toxins and other bacterial proteins suggests that the PTSAgs evolved through the recombination of two smaller β-strand motifs.

Original languageEnglish (US)
Pages (from-to)520-531
Number of pages12
JournalJournal of Molecular Evolution
Volume51
Issue number6
DOIs
StatePublished - 2000

Keywords

  • Enterotoxins
  • MHC class II
  • Protein conformation
  • Staphylococcus aureus
  • T-cell receptor
  • Toxic shock syndrome toxin-1

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