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Protein Science (2003), 12:379-383.
Copyright © 2003 The Protein Society

FOR THE RECORD

Vibrio cholerae cytolysin is composed of an {alpha}-hemolysin-like core

Rich Olson1 and Eric Gouaux1,2

1 Department of Biochemistry and Molecular Biophysics
2 Howard Hughes Medical Institute, Columbia University, New York, New York 10032, USA

Reprint requests to: Eric Gouaux, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; e-mail: jeg52{at}columbia.edu; fax: (212) 305-8174.

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.

Keywords: {alpha}-hemolysin; cytolysin; lectin; leukocidin; pore-forming bacterial toxins; ricin; Staphylococcus aureus; Vibrio cholerae

Abbreviations: VCC, Vibrio cholerae cytolysin • {alpha}HL, {alpha}-hemolysin • LukF, leukocidin F component


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