STRUCTURE AND FUNCTION OF PNEUMOLYSIN, THE MULTIFUNCTIONAL, THIOL-ACTIVATED TOXIN OF STREPTOCOCCUS-PNEUMONIAE

被引：115

作者：

BOULNOIS, GJ ^{[1
]}

PATON, JC ^{[1
]}

MITCHELL, TJ ^{[1
]}

ANDREW, PW ^{[1
]}

机构：

[1] ADELPHI UNIV,DEPT MICROBIOL,GARDEN CITY,NY 11530

来源：

MOLECULAR MICROBIOLOGY | 1991年 / 5卷 / 11期

基金：

英国惠康基金;

关键词：

D O I：

10.1111/j.1365-2958.1991.tb01969.x

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 is a thiol-activated, membrane-damaging, multifunctional toxin and a known virulence factor of Streptococcus pneumoniae. The toxin can interfere with the functioning of both cellular and soluble components of the human immune system which protects against pneumococcal infection. Different amino acids within the toxin which are important in promoting oligomerization of the toxin in membranes and for the generation of functional lesions have been identified by site-directed mutagenesis. Pneumolysin can also activate the classical pathway of complement, and this appears to involve antibody binding (via Fc) by a region of the toxin homologous to C-reactive protein, a human acute-phase protein also capable of classical pathway activation and implicated in host defence against pneumococcal infection.

引用

页码：2611 / 2616

页数：6

共 47 条

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