Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core |
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| Authors: | Olson Rich Gouaux Eric |
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| Affiliation: | Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA. |
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| 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 alpha-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 alpha-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. |
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| Keywords: | α-hemolysin cytolysin lectin leukocidin pore-forming bacterial toxins ricin Staphylococcus aureus Vibrio cholerae |
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