A close-up of the chaperone–usher pilus


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Access through your institution Buy or subscribe Chaperone–usher pili are found on many bacterial pathogens; for example, in uropathogenic _Escherichia coli_, they are involved in adhesion


to host tissues and biofilm formation. Hospenthal _et al_. now provide a detailed look at the composition of the pilus rod from individual subunits in a 3.8 Å resolution cryoelectron


microscopy reconstruction. Each subunit interacts with five preceding and five succeeding subunits, forming the helical rod. Interestingly, almost half of the surface area of each subunit


contacts other subunits and mutations in central positions of these contacting interfaces impair rod formation. Amino-terminal extensions, 10-20 residues long, provide strong hydrophobic


interactions between neighbouring subunits. Furthermore, the subunits also interface through weak polar interactions, in particular between subunits not directly next to each other. This


combination of strong and weak interactions enables partial uncoiling of the rod — for example, to withstand the shear forces of urinary flow — while retaining the structural integrity


needed to keep the bacteria attached. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive


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REFERENCES * Hospenthal, M. K. et al. Structure of a chaperone-usher pilus reveals the molecular basis of rod uncoiling. _Cell_ http://dx.doi.org/10.1016/j.cell.2015.11.049 (2015) Download


references Authors * Ursula Hofer View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE


THIS ARTICLE Hofer, U. A close-up of the chaperone–usher pilus. _Nat Rev Microbiol_ 14, 65 (2016). https://doi.org/10.1038/nrmicro.2016.5 Download citation * Published: 19 January 2016 *


Issue Date: February 2016 * DOI: https://doi.org/10.1038/nrmicro.2016.5 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link


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