Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus

Sumio Shinoda; Kazuhiko Ishida; Eun‐Gyoung ‐G Oh; Kazuhiro Sasahara; Shin‐Ichi ‐I Miyoshi; Mohammad Afzalur Rahim Chowdhury; Tatsuji Yasuda

doi:10.1111/j.1348-0421.1993.tb03229.x

Studies on Hemolytic Action of a Hemolysin Produced by Vibrio mimicus

Sumio Shinoda, Kazuhiko Ishida, Eun‐Gyoung ‐G Oh, Kazuhiro Sasahara, Shin‐Ichi ‐I Miyoshi, Mohammad Afzalur Rahim Chowdhury, Tatsuji Yasuda

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

37 Citations (Scopus)

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)	405-409
Number of pages	5
Journal	MICROBIOLOGY and IMMUNOLOGY
Volume	37
Issue number	5
DOIs	https://doi.org/10.1111/j.1348-0421.1993.tb03229.x
Publication status	Published - May 1993

Keywords

gangliosides
hemolysin
vibrio mimicus

ASJC Scopus subject areas

Microbiology
Immunology
Virology

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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.",

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author = "Sumio Shinoda and Kazuhiko Ishida and Oh, {Eun‐Gyoung ‐G} and Kazuhiro Sasahara and Miyoshi, {Shin‐Ichi ‐I} and Chowdhury, {Mohammad Afzalur Rahim} and Tatsuji Yasuda",

year = "1993",

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doi = "10.1111/j.1348-0421.1993.tb03229.x",

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AU - Shinoda, Sumio

AU - Ishida, Kazuhiko

AU - Oh, Eun‐Gyoung ‐G

AU - Sasahara, Kazuhiro

AU - Miyoshi, Shin‐Ichi ‐I

AU - Chowdhury, Mohammad Afzalur Rahim

AU - Yasuda, Tatsuji

PY - 1993/5

Y1 - 1993/5

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.

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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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