Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus

Sumin Shinnda; Kazuhiko Ishida; Eun Gyoung Oh; Kazuhiro Sasahara; Shin ichi Miyoshi; Mohammad Afzalur Rahim Chowdhurv; Tatsuji Yasuda

Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus

Sumin Shinnda, Kazuhiko Ishida, Eun Gyoung Oh, Kazuhiro Sasahara, Shin ichi Miyoshi, Mohammad Afzalur Rahim Chowdhurv, Tatsuji Yasuda

Research output: Contribution to journal › Article › peer-review

Abstract

Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca²⁺, Mg²⁺ and Mn²+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.

Original language	English
Pages (from-to)	774-777
Number of pages	4
Journal	MICROBIOLOGY and IMMUNOLOGY
Volume	37
Issue number	5
Publication status	Published - Jan 1 1993

Keywords

Gangliosides
Hemolysin
Vibrio mimicus

ASJC Scopus subject areas

Microbiology
Immunology
Virology

Cite this

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title = "Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus",

abstract = "Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca2+, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.",

keywords = "Gangliosides, Hemolysin, Vibrio mimicus",

author = "Sumin Shinnda and Kazuhiko Ishida and Oh, {Eun Gyoung} and Kazuhiro Sasahara and Miyoshi, {Shin ichi} and {Rahim Chowdhurv}, {Mohammad Afzalur} and Tatsuji Yasuda",

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T1 - Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus

AU - Shinnda, Sumin

AU - Ishida, Kazuhiko

AU - Oh, Eun Gyoung

AU - Sasahara, Kazuhiro

AU - Miyoshi, Shin ichi

AU - Rahim Chowdhurv, Mohammad Afzalur

AU - Yasuda, Tatsuji

PY - 1993/1/1

Y1 - 1993/1/1

N2 - Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca2+, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.

AB - Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-labile and inhibited by addition of divalent cations, including Ca2+, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.

KW - Gangliosides

KW - Hemolysin

KW - Vibrio mimicus

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Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus

Abstract

Keywords

ASJC Scopus subject areas

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