Vibrio cholerae cytolysin is composed of an α-hemolysin-like core

Rich Olson, Eric Gouaux

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


The enteric pathogen Vibrio cholerae secretes a water-soluble 80-kD cytolysin, Vibrio cholerae cytolysin (VCC) that assembles into pentameric channels following proteolytic activation by exogenous proteases. Until now, VCC has been placed in a unique class of pore-forming toxins, distinct from paradigms such as Staphyloccal α-hemolysin. However, as reported here, amino acid sequence analysis and three-dimensional structure modeling indicate that the core component of the VCC toxin is related in sequence and structure to a family of hemolysins from Staphylococcus aureus that include leukocidin F and α-hemolysin. Furthermore, our analysis has identified the channel-forming region of VCC and a potential lipid head-group binding site, and suggests a conserved mechanism of assembly and lysis. An additional domain in the VCC toxin is related to plant lectins, conferring additional target cell specificity to the toxin.

Original languageEnglish (US)
Pages (from-to)379-383
Number of pages5
JournalProtein Science
Issue number2
StatePublished - Feb 1 2003
Externally publishedYes


  • Cytolysin
  • Lectin
  • Leukocidin
  • Pore-forming bacterial toxins
  • Ricin
  • Staphylococcus aureus
  • Vibrio cholerae
  • α-hemolysin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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