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Molecular mechanism of bacterial type 1 and P pili assembly
Author(s) -
Andreas Busch,
Gilles Phan,
Gabriel Waksman
Publication year - 2015
Publication title -
philosophical transactions of the royal society a mathematical physical and engineering sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.074
H-Index - 169
eISSN - 1471-2962
pISSN - 1364-503X
DOI - 10.1098/rsta.2013.0153
Subject(s) - pilus , periplasmic space , chaperone (clinical) , fimbria , biogenesis , bacterial outer membrane , fimbriae proteins , biology , microbiology and biotechnology , molecular machine , computational biology , escherichia coli , genetics , gene , medicine , pathology
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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