Pore-forming toxins: ancient, but never really out of fashion

被引:561
作者
Dal Peraro, Matteo [1 ]
van der Goot, F. Gisou [2 ]
机构
[1] Ecole Polytech Fed Lausanne, Sch Life Sci, Inst Bioengn, CH-1015 Lausanne, Switzerland
[2] Ecole Polytech Fed Lausanne, Sch Life Sci, Global Hlth Inst, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
CHOLESTEROL-DEPENDENT CYTOLYSIN; VIBRIO-CHOLERAE CYTOLYSIN; PERFRINGENS EPSILON-TOXIN; ESCHERICHIA-COLI HEMOLYSIN; MEMBRANE-SPANNING DOMAIN; RAY CRYSTAL-STRUCTURE; EQUINATOXIN-II; STRUCTURAL BASIS; ALPHA-HEMOLYSIN; X-RAY;
D O I
10.1038/nrmicro.2015.3
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Pore-forming toxins (PFTs) are virulence factors produced by many pathogenic bacteria and have long fascinated structural biologists, microbiologists and immunologists. Interestingly, pore-forming proteins with remarkably similar structures to PFTs are found in vertebrates and constitute part of their immune system. Recently, structural studies of several PFTs have provided important mechanistic insights into the metamorphosis of PFTs from soluble inactive monomers to cytolytic transmembrane assemblies. In this Review, we discuss the diverse pore architectures and membrane insertion mechanisms that have been revealed by these studies, and we consider how these features contribute to binding specificity for different membrane targets. Finally, we explore the potential of these structural insights to enable the development of novel therapeutic strategies that would prevent both the establishment of bacterial resistance and an excessive immune response.
引用
收藏
页码:77 / 92
页数:16
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