Pore formation: An ancient yet complex form of attack

被引:137
作者
Iacovache, Ioan [1 ]
van der Goot, F. Gisou [1 ]
Pernot, Lucile [1 ]
机构
[1] Ecole Polytech Fed Lausanne, Global Hlth Inst, Fac Life Sci, CH-1015 Lausanne, Switzerland
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2008年 / 1778卷 / 7-8期
关键词
pore-forming toxin; perforin; cholesterol-dependent cytolysin; aerolysin; actinoporin;
D O I
10.1016/j.bbamem.2008.01.026
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
Bacteria, as well as higher organisms such as sea anemones or earthworms, have developed sophisticated virulence factors such as the pore-forming toxins (PFTs) to mount their attack against the host. One of the most fascinating aspects of PFTs is that they can adopt a water-soluble form at the beginning of their lifetime and become an integral transmembrane protein in the membrane of the target cells. There is a growing understanding of the sequence of events and the various conformational changes undergone by these toxins in order to bind to the host cell surface, to penetrate the cell membranes and to achieve pore formation. These points will be addressed in this review. (c) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:1611 / 1623
页数:13
相关论文
共 145 条
[1]   The glycan core of GPI-anchored proteins modulates aerolysin binding but is not sufficient: the polypeptide moiety is required for the toxin-receptor interaction [J].
Abrami, L ;
Velluz, MC ;
Hong, YJ ;
Ohishi, K ;
Mehlert, A ;
Ferguson, M ;
Kinoshita, T ;
van der Goot, FG .
FEBS LETTERS, 2002, 512 (1-3) :249-254
[2]   The pore-forming toxin proaerolysin is activated by furin [J].
Abrami, L ;
Fivaz, M ;
Decroly, E ;
Seidah, NG ;
Jean, F ;
Thomas, G ;
Leppla, SH ;
Buckley, JT ;
van der Goot, FG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (49) :32656-32661
[3]   Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin [J].
Abrami, L ;
van der Goot, FG .
JOURNAL OF CELL BIOLOGY, 1999, 147 (01) :175-184
[4]   Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II [J].
Alegre-Cebollada, Jorge ;
del Pozo, Alvaro Martinez ;
Gavilanes, Jose G. ;
Goormaghtigh, Erik .
BIOPHYSICAL JOURNAL, 2007, 93 (09) :3191-3201
[5]   Lipids favoring inverted phase enhance the ability of aerolysin to permeabilize liposome bilayers [J].
Alonso, A ;
Goñi, FM ;
Buckley, JT .
BIOCHEMISTRY, 2000, 39 (46) :14019-14024
[6]  
Alouf J.E., 2005, The Comprehensive Sourcebook of Bacterial Protein Toxins
[7]   Interaction of the eukaryotic pore-forming cytolysin equinatoxin II with model membranes:: 19F NMR studies [J].
Anderluh, G ;
Razpotnik, A ;
Podlesek, Z ;
Macek, P ;
Separovic, F ;
Norton, RS .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (01) :27-39
[8]   A natively unfolded toxin domain uses its receptor as a folding template [J].
Anderluh, G ;
Gökçe, I ;
Lakey, JH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (21) :22002-22009
[9]   Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures [J].
Anderluh, G ;
Dalla Serra, M ;
Viero, G ;
Guella, G ;
Macek, P ;
Menestrina, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (46) :45216-45223
[10]   Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA [J].
Anderluh, G ;
Hong, Q ;
Boetzel, R ;
MacDonald, C ;
Moore, GR ;
Virden, R ;
Lakey, JH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (24) :21860-21868