Difference in cholesterol-binding and cytolytic activities between listeriolysin O and seeligeriolysin O: a possible role of alanine residue in tryptophan-rich undecapeptide

被引:10
作者
Ito, Y
Kawamura, I
Kohda, C
Baba, H
Kimoto, T
Watanabe, I
Nomura, T
Mitsuyama, M
机构
[1] Kyoto Univ, Grad Sch Med, Dept Microbiol, Sakyo Ku, Kyoto 6068501, Japan
[2] Nagoya Univ, Sch Med, Dept Internal Med 1, Nagoya, Aichi 4668550, Japan
基金
日本学术振兴会;
关键词
listeriolysin O; seeligeriolysin O; undecapeptide; cholesterol bindings; cytolysis;
D O I
10.1016/S0378-1097(01)00349-4
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
We have constructed recombinant listeriolysin O (rLLO) and seeligeriolysin O (rLSO) from Listeria monocytogenes and Listeria seeligeri, respectively. In hemolysis and cholesterol-binding assays, the specific activity of recombinant toxin was lower for LSO as compared to LLO. To understand the molecular basis of this difference, in particular with respect to the conserved Trp-rich undecapeptide, a naturally occurring Ala To Phe substitution in LSO was introduced into rLLO. The rLLO:A488F hemolysin exhibited a reduced activity in both hemolysis and cholesterol-binding. The reverse mutation, inserted into rLSO, also increased the hemolytic activity of this mutant LSO. These results suggested that the natural replacement of Ala to Phe is involved in the weak cytolytic activity of LSO. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:185 / 189
页数:5
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