Some properties of nicked Vibrio vulnificus hemolysin

Vibrio vulnificus, an opportunistic human pathogen, secretes the 50 kDa single-chain hemolysin. When incubated with an exocellular protease from this vibrio, the 50 kDa hemolysin was cleaved in some peptides joined with the disulfide bond(s); the 40 kDa fragment and the small fragment(s) undetectabl...

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Bibliographic Details
Published in:Microbial pathogenesis 1997-10, Vol.23 (4), p.235-239
Main Authors: MIYOSHI, S.-I, FUJII, S, TOMOCHIKA, K.-I, SHINODA, S
Format: Article
Language:English
Subjects:
Bacterial Proteins
Bacteriology
Biological and medical sciences
Endopeptidases - metabolism
Fundamental and applied biological sciences. Psychology
Hemolysin Proteins - immunology
Hemolysin Proteins - pharmacology
Hemolysis
Immunodiffusion
Microbiology
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Peptide Fragments - immunology
Peptide Fragments - pharmacology
Vibrio - enzymology
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Summary:Vibrio vulnificus, an opportunistic human pathogen, secretes the 50 kDa single-chain hemolysin. When incubated with an exocellular protease from this vibrio, the 50 kDa hemolysin was cleaved in some peptides joined with the disulfide bond(s); the 40 kDa fragment and the small fragment(s) undetectable in SDS-PAGE. The nicked hemolysin induced comparable hemolysis through the same process as that of the intact toxin. However, the nicked hemolysin was found to be more stable against inactivation due to autoaggregation, so that it formed a larger precipitation zone in the single radial immunodiffusion test using the antiserum against the intact hemolysin. These results suggest that V. vulnificus hemolysin is modified to be a more hydrophilic protein by nicking, while it is not accompanied by loss of the hemolytic activity.
ISSN:0882-4010
1096-1208
DOI:10.1006/mpat.1997.0149