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Applied and Environmental Microbiology, August 2001, p. 3707-3711, Vol. 67, No. 8
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.8.3707-3711.2001

Purification and Characterization of a Vulnificolysin-Like Cytolysin Produced by Vibrio tubiashii

Mahendra H. Kothary,^1,* Rachel B. Delston,² Sherill K. Curtis,² Barbara A. McCardell,¹ and Ben D. Tall²

Divisions of Virulence Assessment¹ and Microbiological Studies,² Center for Food Safety and Applied Nutrition, U.S. Food and Drug Administration, Washington, D.C. 20204

Received 15 February 2001/Accepted 15 May 2001

An extracellular cytolysin from Vibrio tubiashii was purified by sequential hydrophobic interaction chromatography with phenyl-Sepharose CL-4B and gel filtration with Sephacryl S-200. This protein is sensitive to heat and proteases, is inhibited by cholesterol, and has a molecular weight of 59,000 and an isoelectric point of 5.3. In addition to lysing various erythrocytes, it is cytolytic and/or cytotoxic to Chinese hamster ovary cells, Caco-2 cells, and Atlantic menhaden liver cells in tissue culture. Lysis of erythrocytes occurs by a multihit process that is dependent on temperature and pH. Twelve of the first 17 N-terminal amino acid residues (Asp-Asp-Tyr-Val-Pro-Val-Val-Glu-Lys-Val-Tyr-Tyr-Ile-Thr-Ser-Ser-Lys) are identical to those of the Vibrio vulnificus cytolysin.

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^* Corresponding author. Mailing address: Division of Virulence Assessment (HFS-327), Center for Food Safety and Applied Nutrition, U.S. Food and Drug Administration, 200 C Street, S.W., Washington, DC 20204. Phone: (202) 205-4454. Fax: (202) 205-4939. E-mail: mkothary{at}cfsan.fda.gov.

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Applied and Environmental Microbiology, August 2001, p. 3707-3711, Vol. 67, No. 8
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.8.3707-3711.2001

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