Protein secretion systems in Pseudomonas aeruginosa: an essay on diversity, evolution, and function

被引:130
作者
Filloux, Alain [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, Ctr Mol Microbiol & Infect, London SW7 2AZ, England
来源
FRONTIERS IN MICROBIOLOGY | 2011年 / 2卷
基金
英国惠康基金;
关键词
cell envelope; nanomachine; macromolecular complex; channel; targeting;
D O I
10.3389/fmicb.2011.00155
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Protein secretion systems are molecular nanomachines used by Gram-negative bacteria to thrive within their environment. They are used to release enzymes that hydrolyze complex carbon sources into usable compounds, or to release proteins that capture essential ions such as iron. They are also used to colonize and survive within eukaryotic hosts, causing acute or chronic infections, subverting the host cell response and escaping the immune system. In this article, the opportunistic human pathogen Pseudomonas aeruginosa is used as a model to review the diversity of secretion systems that bacteria have evolved to achieve these goals. This diversity may result from a progressive transformation of cell envelope complexes that initially may not have been dedicated to secretion. The striking similarities between secretion systems and type IV pili, flagella, bacteriophage tail, or efflux pumps is a nice illustration of this evolution. Differences are also needed since various secretion configurations call for diversity. For example, some proteins are released in the extracellular medium while others are directly injected into the cytosol of eukaryotic cells. Some proteins are folded before being released and transit into the periplasm. Other proteins cross the whole cell envelope at once in an unfolded state. However, the secretion system requires conserved basic elements or features. For example, there is a need for an energy source or for an outer membrane channel. The structure of this review is thus quite unconventional. Instead of listing secretion types one after each other, it presents a melting pot of concepts indicating that secretion types are in constant evolution and use basic principles. In other words, emergence of new secretion systems could be predicted the way Mendeleiev had anticipated characteristics of yet unknown elements.
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页数:21
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共 250 条
[11]   A novel type 11 secretion system in Pseudomonas aeruginosa [J].
Ball, G ;
Durand, É ;
Lazdunski, A ;
Filloux, A .
MOLECULAR MICROBIOLOGY, 2002, 43 (02) :475-485
[12]   Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa [J].
Ball, G ;
Chapon-Hervé, V ;
Bleves, S ;
Michel, G ;
Bally, M .
JOURNAL OF BACTERIOLOGY, 1999, 181 (02) :382-388
[13]   In vitro self-assembly from a simple protein of tailorable nanotubes building block [J].
Ballister, Edward R. ;
Lai, Angela H. ;
Zuckermann, Ronald N. ;
Cheng, Yifan ;
Mougous, Joseph D. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (10) :3733-3738
[14]   PROTEIN SECRETION IN PSEUDOMONAS-AERUGINOSA - CHARACTERIZATION OF 7 XCP GENES AND PROCESSING OF SECRETORY APPARATUS COMPONENTS BY PREPILIN PEPTIDASE [J].
BALLY, M ;
FILLOUX, A ;
AKRIM, M ;
BALL, G ;
LAZDUNSKI, A ;
TOMMASSEN, J .
MOLECULAR MICROBIOLOGY, 1992, 6 (09) :1121-1131
[15]   PROTEIN SECRETION IN PSEUDOMONAS-AERUGINOSA - THE XCPA GENE ENCODES AN INTEGRAL INNER MEMBRANE-PROTEIN HOMOLOGOUS TO KLEBSIELLA-PNEUMONIAE SECRETION FUNCTION PROTEIN PULO [J].
BALLY, M ;
BALL, G ;
BADERE, A ;
LAZDUNSKI, A .
JOURNAL OF BACTERIOLOGY, 1991, 173 (02) :479-486
[16]   Patatin-like proteins: a new family of lipolytic enzymes present in bacteria? [J].
Banerji, S ;
Flieger, A .
MICROBIOLOGY-SGM, 2004, 150 :522-525
[17]   A novel extracellular phospholipase C of Pseudomonas aeruginosa is required for phospholipid chemotaxis [J].
Barker, AP ;
Vasil, AI ;
Filloux, A ;
Ball, G ;
Wilderman, PJ ;
Vasil, ML .
MOLECULAR MICROBIOLOGY, 2004, 53 (04) :1089-1098
[18]   3-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS-AERUGINOSA - A 2-DOMAIN PROTEIN WITH A CALCIUM-BINDING PARALLEL-BETA ROLL MOTIF [J].
BAUMANN, U ;
WU, S ;
FLAHERTY, KM ;
MCKAY, DB .
EMBO JOURNAL, 1993, 12 (09) :3357-3364
[19]   A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A [J].
Benabdelhak, H ;
Kiontke, S ;
Horn, C ;
Ernst, R ;
Blight, MA ;
Holland, IB ;
Schmitt, L .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 327 (05) :1169-1179
[20]   Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates:: Evidence for a possible association between O serotypes and exo genes [J].
Berthelot, P ;
Attree, I ;
Plésiat, P ;
Chabert, J ;
de Bentzmann, S ;
Pozzetto, B ;
Grattard, F .
JOURNAL OF INFECTIOUS DISEASES, 2003, 188 (04) :512-518