Affiliation:
1. Department of Biological Chemistry, Walter Reed Army Institute of Research, Washington, D.C. 20012
Abstract
Shiga toxin has been purified in milligram quantities to near homogeneity from cell lysates of
Shigella dysenteriae
1 strain 3818-0. Purification involved an initial ultracentrifugation, ammonium sulfate fractionation, chromatography on DEAE-cellulose and carboxymethyl cellulose, gel filtration, and preparative isoelectric focusing in sucrose gradients. The purified toxin was resolved by discontinuous polyacrylamide gel electrophoresis into a major cytotoxic protein band and a closely migrating, cytotoxic protease-nicked minor band. Antiserum generated by immunization with glutaraldehyde-inactivated toxin was shown to be monospecific against
S. dysenteriae
cell lysates. This highly purified toxin was cytotoxic to HeLa cells, enterotoxic in rabbit ileal loops, and lethal to mice. Monospecific antiserum to the toxin neutralized completely these toxin activities in both purified toxin preparations and crude shigella cell lysates.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
81 articles.
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