Abstract
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 language | English (US) |
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Pages (from-to) | 379-383 |
Number of pages | 5 |
Journal | Protein Science |
Volume | 12 |
Issue number | 2 |
DOIs | |
State | Published - Feb 1 2003 |
Externally published | Yes |
Keywords
- Cytolysin
- Lectin
- Leukocidin
- Pore-forming bacterial toxins
- Ricin
- Staphylococcus aureus
- Vibrio cholerae
- α-hemolysin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology