Work

Ordered and Ushered; the Assembly and Translocation of the Adhesive Type I and P Pili

Year: 2013

Type: article

Abstract: Type I and P pili are chaperone-usher pili of uropathogenic Escherichia coli, which allow bacteria to adhere to host cell receptors. Pilus formation and secretion are orchestrated by two accessory proteins, a chaperone, which catalyses pilus subunit folding and maintains them in a polymerization-competent state, and an outer membrane-spanning nanomachine, the usher, which choreographs their assembly into a pilus and drives their secretion through the membrane. In this review, recent structures and kinetic studies are combined to examine the mechanism of type I and P pili assembly, as it is currently known. We also investigate how the knowledge of pilus biogenesis mechanisms has been exploited to design selective inhibitors of the process.

Source: Biology

DOI: 10.3390/biology2030841

Authors: James Lillington, Gabriel Waksman

Institutions: Institute of Structural and Molecular Biology, University College London, Birkbeck, University of London

Language: English

Topic: Biochemical and Structural Characterization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,258

Funders: Medical Research Council, Biotechnology and Biological Sciences Research Council