Molecular mechanism of bacterial type 1 and P pili assembly

被引:26
作者
Busch, Andreas
Phan, Gilles
Waksman, Gabriel [1 ]
机构
[1] UCL, Inst Struct & Mol Biol, London WC1E 7HX, England
来源
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES | 2015年 / 373卷 / 2036期
基金
英国医学研究理事会;
关键词
chaperone-usher; pilus assembly mechanism; host-pathogen interaction; pilicides; DONOR-STRAND EXCHANGE; SUBUNIT COMPLEX RECOGNITION; URINARY-TRACT-INFECTIONS; OUTER-MEMBRANE USHER; STRUCTURAL BASIS; CRYSTAL-STRUCTURE; BIOGENESIS; FIMH; ADHESIN; DOMAIN;
D O I
10.1098/rsta.2013.0153
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
The formation of adhesive surface structures called pili or fimbriae ('bacterial hair') is an important contributor towards bacterial pathogenicity and persistence. To fight often chronic or recurrent bacterial infections such as urinary tract infections, it is necessary to understand the molecular mechanism of the nanomachines assembling such pili. Here, we focus on the so far best-known pilus assembly machinery: the chaperone-usher pathway producing the type 1 and P pili, and highlight the most recently acquired structural knowledge. First, we describe the subunits' structure and the molecular role of the periplasmic chaperone. Second, we focus on the outer-membrane usher structure and the catalytic mechanism of usher-mediated pilus biogenesis. Finally, we describe how the detailed understanding of the chaperone-usher pathway at a molecular level has paved the way for the design of a new generation of bacterial inhibitors called 'pilicides'.
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页数:13
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