Pseudomonas aeruginosa Twitching Motility: Type IV Pili in Action

被引:494
作者
Burrows, Lori L. [1 ]
机构
[1] McMaster Univ, Dept Biochem & Biomed Sci, Michael G DeGroote Inst Infect Dis Res, Hamilton, ON L8N 3Z5, Canada
来源
ANNUAL REVIEW OF MICROBIOLOGY, VOL 66 | 2012年 / 66卷
基金
加拿大健康研究院;
关键词
pilus; fimbriae; assembly system; secretin; type IVa; type IVb; II SECRETION SYSTEM; ENTEROPATHOGENIC ESCHERICHIA-COLI; CORTICAL PLAQUE-FORMATION; CHP CHEMOSENSORY SYSTEM; NEISSERIA-GONORRHOEAE; MYXOCOCCUS-XANTHUS; PROTEIN-SECRETION; BIOFILM FORMATION; VIBRIO-CHOLERAE; FIMBRIAL BIOGENESIS;
D O I
10.1146/annurev-micro-092611-150055
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Type IV pili (T4P) are one of the most common forms of bacterial and archaeal surface structures, involved in adherence, motility, competence for DNA uptake, and pathogenesis. Pseudomonas aeruginosa has emerged as one of the key model systems for the investigation of T4P structure and function. Although its reputation as a serious nosocomial and opportunistic pathogen is well deserved, its facile growth requirements and the ready availability of molecular tools have allowed for rapid advances in our understanding of how T4P are assembled; their contributions to motility, biofilm formation and virulence; and their complex regulation. This review covers recent findings concerning the three different types of T4P found in P. aeruginosa (type IVa, type IVb, and Tad) and provides details about the modes of translocation mediated by T4aP, the architecture and function of the T4aP assembly system, and the complex regulation of T4aP biogenesis and function.
引用
收藏
页码:493 / 520
页数:28
相关论文
共 177 条
[1]   The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae [J].
Abendroth, J ;
Murphy, P ;
Sandkvist, M ;
Bagdasarian, M ;
Holl, WGJ .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 348 (04) :845-855
[2]   The Role of Twitching Motility in Pseudomonas aeruginosa Exit from and Translocation of Corneal Epithelial Cells [J].
Alarcon, Irania ;
Evans, David J. ;
Fleiszig, Suzanne M. J. .
INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, 2009, 50 (05) :2237-2244
[3]   Diversity of archaeal type IV pilin-like structures [J].
Albers, Sonja-Verena ;
Pohlschroeder, Mecky .
EXTREMOPHILES, 2009, 13 (03) :403-410
[4]   Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa [J].
Alm, RA ;
Bodero, AJ ;
Free, PD ;
Mattick, JS .
JOURNAL OF BACTERIOLOGY, 1996, 178 (01) :46-53
[5]   Identification of two genes with prepilin-like leader sequences involved in type 4 fimbrial biogenesis in Pseudomonas aeruginosa [J].
Alm, RA ;
Mattick, JS .
JOURNAL OF BACTERIOLOGY, 1996, 178 (13) :3809-3817
[6]  
Alm RA, 1996, MOL MICROBIOL, V22, P161
[7]   PilZ domain is part of the bacterial c-di-GMP binding protein [J].
Amikam, D ;
Galperin, MY .
BIOINFORMATICS, 2006, 22 (01) :3-6
[8]   Interaction domains in the Pseudomonas aeruginosa type II secretory apparatus component XcpS (GspF) [J].
Arts, Jorik ;
de Groot, Arjan ;
Ball, Genevieve ;
Durand, Eric ;
El Khattabi, Mohammed ;
Filloux, Alain ;
Tommassen, Jan ;
Koster, Margot .
MICROBIOLOGY-SGM, 2007, 153 :1582-1592
[9]   Novel Proteins That Modulate Type IV Pilus Retraction Dynamics in Pseudomonas aeruginosa [J].
Asikyan, Miranda L. ;
Kus, Julianne V. ;
Burrows, Lori L. .
JOURNAL OF BACTERIOLOGY, 2008, 190 (21) :7022-7034
[10]   Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture [J].
Audette, GF ;
Irvin, RT ;
Hazes, B .
BIOCHEMISTRY, 2004, 43 (36) :11427-11435