Purification and characterization of Staphylococcus aureus FRI 1169 and 587 toxic shock syndrome exotoxins

Hideo Igarashi, Hiroshi Fujikawa, Hiroyuki Usami, Shunichiro Kawabata, Takashi Morita

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Abstract

An exotoxin was purified from a toxic shock toxin (TST)-producing Staphylococcus aureus strain, FRI 1169, and another exotoxin was purified from a pyrogenic exotoxin C (PEC)-producing S. aureus strain, 587. Both strains had been isolated from toxic-shock syndrome patients. The two exotoxins were purified by the same method of ion-exchange chromatography, chromatofocusing, and gel filtration. After purification, those exotoxins gave a line of identity against an anti-TST serum and also were immunologically similar to TST in a double-diffusion test. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, each exotoxin gave a single band with a relative mobility identical to that of the other. Their molecular weights (24,000), isoelectric points (7.0), amino acid compositions, and NH2-terminal amino acid sequences (the first four residues) were identical. Both produced fever and enhanced host susceptibility to lethal exotoxin shock in rabbits, comparable with PEC. These findings show that the two exotoxins are the same protein, which is assumed to be TST. When injected into rabbits, the culture supernatant of strain 587 showed biological activity like that described above, whereas the culture supernatant neutralized with anti-TST immunoglobulin did not. This showed that PEC-producing strain 587 does not produce any toxin with these biological activities in rabbits except TST.

Original languageEnglish
Pages (from-to)175-181
Number of pages7
JournalInfection and Immunity
Volume44
Issue number1
DOIs
Publication statusPublished - 1984

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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