Interaction with a lipid membrane: a key step in bacterial toxins virulence

被引:35
作者
Cabiaux, V [1 ]
Wolff, C [1 ]
Ruysschaert, JM [1 ]
机构
[1] Free Univ Brussels, Chim Phys Macromol Interfaces Lab, B-1050 Brussels, Belgium
关键词
bacterial toxins; structure; membrane;
D O I
10.1016/S0141-8130(97)00078-0
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
Bacterial toxins are secreted as soluble proteins. However, they have to interact with a cell lipid membrane either to permeabilize the cells (pore forming toxins) or to enter into the cytosol to express their enzymatic activity (translocation toxins). The aim of this review is to suggest that the strategies developed by toxins to insert in a lipid membrane is mediated by their structure. Two categories, which contains both pore forming and translocation toxins, are emerging: alpha helical proteins containing hydrophobic domains and beta sheets proteins in which no hydrophobicity can be clearly detected. The first category would rather interact with the membrane through multi-spanning helical domains whereas the second category would form a beta barrel in the membrane. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:285 / 298
页数:14
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