Affiliation:
1. Divisions of Virulence Assessment1 and
2. Microbiological Studies,2 Center for Food Safety and Applied Nutrition, U.S. Food and Drug Administration, Washington, D.C. 20204
Abstract
ABSTRACT
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.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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SOS Publications
Fair Haven N.J
Cited by
30 articles.
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