Essential role of domain 4 of pneumolysin from Streptococcus pneumoniae in cytolytic activity as determined by truncated proteins

被引:34
作者
Baba, H
Kawamura, I
Kohda, C
Nomura, T
Ito, Y
Kimoto, T
Watanabe, I
Ichiyama, S
Mitsuyama, M
机构
[1] Kyoto Univ, Grad Sch Med, Dept Microbiol, Sakyo Ku, Kyoto 6068501, Japan
[2] Kyoto Univ Hosp, Dept Clin Lab Med, Sakyo Ku, Kyoto 6068507, Japan
[3] Nagoya Univ, Sch Med, Dept Internal Med 1, Showa Ku, Nagoya, Aichi 4668550, Japan
基金
日本学术振兴会;
关键词
pneumoylsin; Streptococcus pneumoniae; cytolytic activity; hemolysis; membrane cholesterol; thiol-activated cytolysins;
D O I
10.1006/bbrc.2001.4297
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Pneumolysin (PLY), an important virulence factor of Streptococcus pneumoniae, is one of the members of thiol-activated cytolysins (TACYs) consisting of four domains. TACYs commonly bind to membrane cholesterol and oligomerize to form transmembrane pore. We have constructed full-length and various truncated PLYs to study the role of domains of PLY in the cytolytic activity. Full-length PLY had binding ability to both cell membrane and immobilized cholesterol. A truncated PLY which comprised only domain 4 molecule, the C-terminal domain of PLY, sustained the binding ability to cell membrane and cholesterol, whereas domain 1-3 molecule had no binding ability to them. Furthermore, the domain 4 molecule inhibited both the membrane binding and the hemolytic activity of full-length PLY. Accordingly, the present results provided the direct evidence that domain 4 was essential for the initial binding to membrane cholesterol and the interaction led to the subsequent membrane damage process. (C) 2001 Academic Press.
引用
收藏
页码:37 / 44
页数:8
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