Hemolytic mechanism of cytolysin produced from V. vulnificus

Hyung Rho Kim; Hye Won Rho; Mi Hee Jeong; Jin Woo Park; Jong Suk Kim; Byung Hyun Park; Uh Hyun Kim; Seok Don Park

doi:10.1016/0024-3205(93)90714-E

Hemolytic mechanism of cytolysin produced from V. vulnificus

Hyung Rho Kim
, Hye Won Rho
, Mi Hee Jeong
, Jin Woo Park
, Jong Suk Kim
, Byung Hyun Park
, Uh Hyun Kim
, Seok Don Park

Department of Medicine

Jeonbuk National University
Wonkwang University

Research output: Contribution to journal › Journal article › peer-review

65 Scopus citations

Abstract

The characteristics of hemolytic action of cytolysin produced from V. vulnificus were investigated in mouse erythrocytes. The cytolysin bound erythrocyte membranes in temperature-independent manner and then lysed cells temperature-dependently. Hemoglobin release by the cytolysin was completely inhibited by the presence of raffinose or melezitose, but K⁺ release was not affected. The cytolysin-induced hemolysis was always accompanied with the conversion of membrane-bound cytolysin into an oligomer of 210 kDa, corresponding to a tetramer of native cytolysins. Nonesterified cholesterol inactivated the cytolysin by converting active monomeric cytolysin into inactive oligomer. The results suggest that the cytolysin lyses erythrocytes due to the formation of small pores on erythrocyte membrane by cholesterol-mediated oligomerization of the cytolysin.

Original language	English
Pages (from-to)	571-577
Number of pages	7
Journal	Life Sciences
Volume	53
Issue number	7
DOIs	https://doi.org/10.1016/0024-3205(93)90714-E
State	Published - 1993

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@article{a13e83d76658485195f77fed6b21c2c0,

title = "Hemolytic mechanism of cytolysin produced from V. vulnificus",

abstract = "The characteristics of hemolytic action of cytolysin produced from V. vulnificus were investigated in mouse erythrocytes. The cytolysin bound erythrocyte membranes in temperature-independent manner and then lysed cells temperature-dependently. Hemoglobin release by the cytolysin was completely inhibited by the presence of raffinose or melezitose, but K+ release was not affected. The cytolysin-induced hemolysis was always accompanied with the conversion of membrane-bound cytolysin into an oligomer of 210 kDa, corresponding to a tetramer of native cytolysins. Nonesterified cholesterol inactivated the cytolysin by converting active monomeric cytolysin into inactive oligomer. The results suggest that the cytolysin lyses erythrocytes due to the formation of small pores on erythrocyte membrane by cholesterol-mediated oligomerization of the cytolysin.",

author = "Kim, \{Hyung Rho\} and Rho, \{Hye Won\} and Jeong, \{Mi Hee\} and Park, \{Jin Woo\} and Kim, \{Jong Suk\} and Park, \{Byung Hyun\} and Kim, \{Uh Hyun\} and Park, \{Seok Don\}",

year = "1993",

doi = "10.1016/0024-3205(93)90714-E",

language = "English",

volume = "53",

pages = "571--577",

journal = "Life Sciences",

issn = "0024-3205",

number = "7",

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TY - JOUR

T1 - Hemolytic mechanism of cytolysin produced from V. vulnificus

AU - Kim, Hyung Rho

AU - Rho, Hye Won

AU - Jeong, Mi Hee

AU - Park, Jin Woo

AU - Kim, Jong Suk

AU - Park, Byung Hyun

AU - Kim, Uh Hyun

AU - Park, Seok Don

PY - 1993

Y1 - 1993

N2 - The characteristics of hemolytic action of cytolysin produced from V. vulnificus were investigated in mouse erythrocytes. The cytolysin bound erythrocyte membranes in temperature-independent manner and then lysed cells temperature-dependently. Hemoglobin release by the cytolysin was completely inhibited by the presence of raffinose or melezitose, but K+ release was not affected. The cytolysin-induced hemolysis was always accompanied with the conversion of membrane-bound cytolysin into an oligomer of 210 kDa, corresponding to a tetramer of native cytolysins. Nonesterified cholesterol inactivated the cytolysin by converting active monomeric cytolysin into inactive oligomer. The results suggest that the cytolysin lyses erythrocytes due to the formation of small pores on erythrocyte membrane by cholesterol-mediated oligomerization of the cytolysin.

AB - The characteristics of hemolytic action of cytolysin produced from V. vulnificus were investigated in mouse erythrocytes. The cytolysin bound erythrocyte membranes in temperature-independent manner and then lysed cells temperature-dependently. Hemoglobin release by the cytolysin was completely inhibited by the presence of raffinose or melezitose, but K+ release was not affected. The cytolysin-induced hemolysis was always accompanied with the conversion of membrane-bound cytolysin into an oligomer of 210 kDa, corresponding to a tetramer of native cytolysins. Nonesterified cholesterol inactivated the cytolysin by converting active monomeric cytolysin into inactive oligomer. The results suggest that the cytolysin lyses erythrocytes due to the formation of small pores on erythrocyte membrane by cholesterol-mediated oligomerization of the cytolysin.

UR - https://www.scopus.com/pages/publications/0027320947

U2 - 10.1016/0024-3205(93)90714-E

DO - 10.1016/0024-3205(93)90714-E

M3 - Journal article

C2 - 8350671

AN - SCOPUS:0027320947

SN - 0024-3205

VL - 53

SP - 571

EP - 577

JO - Life Sciences

JF - Life Sciences

IS - 7

ER -

Hemolytic mechanism of cytolysin produced from V. vulnificus

Abstract

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