Take five - Type VII secretion systems of Mycobacteria

被引:145
|
作者
Houben, Edith N. G. [1 ,2 ]
Korotkov, Konstantin V. [3 ]
Bitter, Wilbert [1 ,2 ]
机构
[1] Vrije Univ Amsterdam, NL-1081 HV Amsterdam, Netherlands
[2] Vrije Univ Amsterdam, Med Ctr, NL-1081 HV Amsterdam, Netherlands
[3] Univ Kentucky, Lexington, KY USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2014年 / 1843卷 / 08期
关键词
Protein secretion; Mycobacterium; Secretion signal; Chaperone; Protease; VIRULENCE FACTOR SECRETION; OUTER-MEMBRANE; PROTEIN SECRETION; ESX-1; SECRETION; TUBERCULOSIS VIRULENCE; CRYSTAL-STRUCTURE; CALMETTE-GUERIN; GENE-CLUSTER; DNA TRANSFER; ESAT-6;
D O I
10.1016/j.bbamcr.2013.11.003
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
Mycobacteria use type VII secretion (T7S) systems to secrete proteins across their complex cell envelope. Pathogenic mycobacteria, such as the notorious pathogen Mycobacterium tuberculosis, have up to five of these secretion systems, named ESX-1 to ESX-5. At least three of these secretion systems are essential for mycobacterial virulence and/or viability. Elucidating T7S is therefore essential to understand the success of M. tuberculosis and other pathogenic mycobacteria as pathogens, and could be instrumental to identify novel targets for drug- and vaccine-development. Recently, significant progress has been achieved in the identification of T7S substrates and a general secretion motif. In addition, a start has been made with unraveling the mechanism of secretion and the structural analysis of the different subunits. This review summarizes these recent findings, which are incorporated in a working model of this complex machinery. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:1707 / 1716
页数:10
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