1987
DOI: 10.1099/00221287-133-10-2853
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Variability of Haemolysin(s) Produced by Vibrio vulnficus

Abstract: The peptide composition and antigenic cross-reactivity of partially purified and concentrated haemolysins of 16 strains of Vibrio vulnificus were examined by SDS-PAGE and immunoblotting analysis, using a monoclonal antibody (MAb), 6F8D, raised against the haemolysin. All strains produced a common peptide of 36 kDa and the MAb reacted with this peptide. In some strains, larger molecules, including a 56 kDa peptide, were produced, but the MAb did not react with this peptide. The haemolytic activity of the strain… Show more

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Cited by 3 publications
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“…The toxin may bind cholesterol and has been shown to induce the release of K+ ions and to a lesser extent Na+ from liposomes (20). Other investigators have reported a possible second hemolysin with an estimated molecular mass of 36 kDa, whose hemolytic activity is neutralized by monoclonal antibody, that binds a 36-kDa protein but not a 56-kDa protein in culture supernatants (12). However, the biological properties of both of these proteins appear to be identical, and the relationship between them is unclear.…”
mentioning
confidence: 99%
“…The toxin may bind cholesterol and has been shown to induce the release of K+ ions and to a lesser extent Na+ from liposomes (20). Other investigators have reported a possible second hemolysin with an estimated molecular mass of 36 kDa, whose hemolytic activity is neutralized by monoclonal antibody, that binds a 36-kDa protein but not a 56-kDa protein in culture supernatants (12). However, the biological properties of both of these proteins appear to be identical, and the relationship between them is unclear.…”
mentioning
confidence: 99%
“…A radiolabeled probe to the VVH gene provides specific confirmation of both environmental and clinical isolates of V. vulnificus (12,21,43). Hemolysin production has been reported in all V. vulnificus isolates tested by numerous investigators, including 12 isolates tested by Johnson and Calia (11), 44 isolates tested by Kaysner et al (12), 16 isolates tested by Morris et al (21), 33 isolates tested by Morris et al (22), 16 isolates tested by Okada et al (25), and 40 isolates tested by Tison and Kelly (38). This research seeks to (i) produce reagent antibodies to VVH, (ii) develop a sandwich enzyme-linked immunosorbent assay (ELISA) for VVH to detect V. vulnificus isolates, and (iii) evaluate the sandwich ELISA as a method for detection and enumeration of V. vulnificus in oysters and other environmental specimens.…”
mentioning
confidence: 99%
“…An antigenic protein, V. vulnificus hemolysin (VVH), is produced in maximal amounts at the mid-to late-exponential growth phase (8,15,25,37). VVH is apparently specific to V. vulnificus.…”
mentioning
confidence: 99%