The ins and outs of Mycobacterium tuberculosis protein export

被引:66
作者
Ligon, Lauren S. [1 ]
Hayden, Jennifer D. [1 ]
Braunstein, Miriam [1 ]
机构
[1] Univ N Carolina, Dept Microbiol & Immunol, Chapel Hill, NC 27599 USA
关键词
Secretion; Sec; SecA2; Tat; ESX; ARGININE TRANSLOCATION PATHWAY; SEC-INDEPENDENT PROTEIN; ESX-1 SECRETION SYSTEM; ESCHERICHIA-COLI; SIGNAL PEPTIDES; PATHOGENIC MYCOBACTERIA; MEMBRANE-PROTEINS; TRANSPORT-SYSTEM; PREPROTEIN TRANSLOCASE; STAPHYLOCOCCUS-AUREUS;
D O I
10.1016/j.tube.2011.11.005
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Mycobacterium tuberculosis is an important pathogen that infects approximately one-third of the world's population and kills almost two million people annually. An important aspect of M. tuberculosis physiology and pathogenesis is its ability to export proteins into and across the thick mycobacterial cell envelope, where they are ideally positioned to interact with the host. In addition to the specific proteins that are exported by M. tuberculosis, the systems through which these proteins are exported represent potential targets for future drug development. M. tuberculosis possesses two well-known and conserved export systems: the housekeeping Sec pathway and the Tat pathway. In addition, M. tuberculosis possesses specialized export systems including the accessory SecA2 pathway and five ESX pathways. Here we review the current understanding of each of these export systems, with a focus on M. tuberculosis, and discuss the contribution of each system to disease and physiology. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:121 / 132
页数:12
相关论文
共 149 条
[11]   Topological studies on the twin-arginine translocase component TatC [J].
Behrendt, J ;
Standar, K ;
Lindenstrauss, U ;
Brüser, T .
FEMS MICROBIOLOGY LETTERS, 2004, 234 (02) :303-308
[12]   Prediction of twin-arginine signal peptides [J].
Bendtsen, JD ;
Nielsen, H ;
Widdick, D ;
Palmer, T ;
Brunak, S .
BMC BIOINFORMATICS, 2005, 6 (1)
[13]   Improved prediction of signal peptides: SignalP 3.0 [J].
Bendtsen, JD ;
Nielsen, H ;
von Heijne, G ;
Brunak, S .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 340 (04) :783-795
[14]   An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets [J].
Bensing, BA ;
Sullam, PM .
MOLECULAR MICROBIOLOGY, 2002, 44 (04) :1081-1094
[15]   A common export pathway for proteins binding complex redox cofactors? [J].
Berks, BC .
MOLECULAR MICROBIOLOGY, 1996, 22 (03) :393-404
[16]   The knockout of the lprG-Rv1410 operon produces strong attenuation of Mycobacterium tuberculosis [J].
Bigi, F ;
Gioffré, A ;
Klepp, L ;
Santangelo, MD ;
Alito, A ;
Caimi, K ;
Meikle, V ;
Zumárraga, M ;
Taboga, O ;
Romano, MI ;
Cataldi, A .
MICROBES AND INFECTION, 2004, 6 (02) :182-187
[17]   Systematic Genetic Nomenclature for Type VII Secretion Systems [J].
Bitter, Wilbert ;
Houben, Edith N. G. ;
Bottai, Daria ;
Brodin, Priscille ;
Brown, Eric J. ;
Cox, Jeffery S. ;
Derbyshire, Keith ;
Fortune, Sarah M. ;
Gao, Lian-Yong ;
Liu, Jun ;
Gey van Pittius, Nicolaas C. ;
Pym, Alexander S. ;
Rubin, Eric J. ;
Sherman, David R. ;
Cole, Stewart T. ;
Brosch, Roland .
PLOS PATHOGENS, 2009, 5 (10)
[18]   An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria [J].
Bogsch, EG ;
Sargent, F ;
Stanley, NR ;
Berks, BC ;
Robinson, C ;
Palmer, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (29) :18003-18006
[19]   SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis [J].
Bordes, Patricia ;
Cirinesi, Anne-Marie ;
Ummels, Roy ;
Sala, Ambre ;
Sakr, Samer ;
Bitter, Wilbert ;
Genevaux, Pierre .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (20) :8438-8443
[20]   Mycobacterial PE, PPE and ESX clusters: novel insights into the secretion of these most unusual protein families [J].
Bottai, Daria ;
Brosch, Roland .
MOLECULAR MICROBIOLOGY, 2009, 73 (03) :325-328