Roles of the carboxy-terminal region of Clostridium perfringens alpha toxin

Masahiro Nagahama, Hiroshi Iida, Eri Nishioka, Keinosuke Okamoto, Jun Sakurai

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

Treatment of Clostridium perfringens alpha toxin with aminopeptidase resulted in no effect on various activities of the toxin. Aminopeptidase did not hydrolyze the native toxin or the toxin treated with urea in the presence of EDTA. Treatment with carboxypeptidase for 30 min resulted in a 75% decrease in these activities. Incubation of the native toxin with carboxypeptidase for 30 min released approximately 15 amino acids from the C-terminus of the toxin. The biological activities of a mutant toxin lacking 20 C-terminal residues of the toxin (AT1-350) showed about 59-87% of the activity of native toxin. The mutant toxin showed partial antigenic identity with the native toxin. These data suggest that the C-terminal domain contributes to maintaining the active form of the toxin.

Original languageEnglish
Pages (from-to)297-301
Number of pages5
JournalFEMS Microbiology Letters
Volume120
Issue number3
DOIs
Publication statusPublished - Jul 15 1994

Keywords

  • Alpha toxin
  • Aminopeptidase
  • C-terminus
  • Carboxypeptidase
  • Clostridium perfringens
  • N-terminus

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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