Structural insights into the biogenesis and biofilm formation by the Escherichia coli common pilus

被引:59
作者
Garnett, James A. [2 ]
Martinez-Santos, Veronica I. [3 ]
Saldana, Zeus [1 ]
Pape, Tillmann [2 ]
Hawthorne, William [2 ]
Chan, Jennifer [2 ]
Simpson, Peter J. [2 ]
Cota, Ernesto [2 ]
Puente, Jose L. [3 ]
Giron, Jorge A. [1 ]
Matthews, Steve [2 ]
机构
[1] Univ Florida, Dept Mol Genet & Microbiol, Emerging Pathogens Inst, Gainesville, FL 32610 USA
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, Struct Biol Ctr, London SW7 2AZ, England
[3] Univ Nacl Autonoma Mexico, Inst Biotecnol, Cuernavaca 62210, Morelos, Mexico
基金
美国国家卫生研究院; 英国惠康基金;
关键词
chaperone-usher; donor-strand exchange; X-ray crystallography; DONOR-STRAND EXCHANGE; ADHERENCE; FIMBRIAE; USHER; FIMH;
D O I
10.1073/pnas.1106733109
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Bacteria have evolved a variety of mechanisms for developing community-based biofilms. These bacterial aggregates are of clinical importance, as they are a major source of recurrent disease. Bacterial surface fibers (pili) permit adherence to biotic and abiotic substrates, often in a highly specific manner. The Escherichia coli common pilus (ECP) represents a remarkable family of extracellular fibers that are associated with both disease-causing and commensal strains. ECP plays a dual role in early-stage biofilm development and host cell recognition. Despite being the most common fimbrial structure, relatively little is known regarding its biogenesis, architecture, and function. Here we report atomic-resolution insight into the biogenesis and architecture of ECP. We also derive a structural model for entwined ECP fibers that not only illuminates interbacteria communication during biofilm formation but also provides a useful foundation for the design of novel nanofibers.
引用
收藏
页码:3950 / 3955
页数:6
相关论文
共 36 条
[1]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[2]   An atomic resolution model for assembly, architecture, and function of the Dr adhesins [J].
Anderson, KL ;
Billington, J ;
Pettigrew, D ;
Cota, E ;
Simpson, P ;
Roversi, P ;
Chen, HA ;
Urvil, P ;
du Merle, L ;
Barlow, PN ;
Medof, ME ;
Smith, RAG ;
Nowicki, B ;
Le Bouguénec, C ;
Lea, SM ;
Matthews, S .
MOLECULAR CELL, 2004, 15 (04) :647-657
[3]   The majority of enteroaggregative Escherichia coli strains produce the E-coli common pilus when adhering to cultured epithelial cells [J].
Avelino, Fabiola ;
Saldana, Zeus ;
Islam, Sohidul ;
Monteiro-Neto, Valerio ;
Dall'Agnol, Monique ;
Eslava, Carlos A. ;
Giron, Jorge A. .
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY, 2010, 300 (07) :440-448
[4]   NarL dimerization?: Suggestive evidence from a new crystal form [J].
Baikalov, I ;
Schröder, I ;
Kaczor-Grzeskowiak, M ;
Cascio, D ;
Gunsalus, RP ;
Dickerson, RE .
BIOCHEMISTRY, 1998, 37 (11) :3665-3676
[5]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[6]   Distribution of the Escherichia coli Common Pilus among Diverse Strains of Human Enterotoxigenic E. coli [J].
Blackburn, Dana ;
Husband, Amanda ;
Saldana, Zeus ;
Nada, Rania A. ;
Klena, John ;
Qadri, Firdausi ;
Giron, Jorge A. .
JOURNAL OF CLINICAL MICROBIOLOGY, 2009, 47 (06) :1781-1784
[7]   X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli [J].
Choudhury, D ;
Thompson, A ;
Stojanoff, V ;
Langermann, S ;
Pinkner, J ;
Hultgren, SJ ;
Knight, SD .
SCIENCE, 1999, 285 (5430) :1061-1066
[8]   Molecular mechanisms of Escherichia coli pathogenicity [J].
Croxen, Matthew A. ;
Finlay, B. Brett .
NATURE REVIEWS MICROBIOLOGY, 2010, 8 (01) :26-38
[9]   Conserved Hydrophobic Clusters on the Surface of the Caf1A Usher C-Terminal Domain Are Important for F1 Antigen Assembly [J].
Dubnovitsky, Anatoly P. ;
Duck, Zoe ;
Kersley, Joanne E. ;
Hard, Torleif ;
MacIntyre, Sheila ;
Knight, Stefan D. .
JOURNAL OF MOLECULAR BIOLOGY, 2010, 403 (02) :243-259
[10]  
ESREY SA, 1991, B WORLD HEALTH ORGAN, V69, P609