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BACTERIAL PHYSIOLOGY

Heads or tails for type V pilus assembly

Nature Microbiology volume 5, pages 782–784 (2020)Cite this article

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Protease-enabled strand exchange to mediate assembly of type V pilus is confirmed using a combination of cryogenic electron microscopy and X-ray crystal structures.

The Gram-negative Bacterioides species are commensal anaerobes from the Bacteroidia class that contribute to the breakdown of high-molecular-weight organic material in the gut1. The class Bacteroidia also includes pathogens such as Porphyromonas gingivalis, which causes severe periodontal disease2. Both pathogenic and commensal Bacteroidetes express adhesins that help them to colonize host niches and interact with host components and other microorganisms in complex biofilms. Among these adhesins are a class of protein filaments called type V pili, which were first identified in the 1980s3 and are assembled by a protease-enabled mechanism at the outer membrane (OM) as shown through structural characterization of the subunits4. Writing in Nature Microbiology, Shibata et al.5 provide atomic-level details of the mechanism of type V pilus assembly and provide three-dimensional context for the binding of these important adhesins to diverse receptors.

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Fig. 1: Comparison of type I and type V pilus assembly.

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  1. Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, Ontario, Canada

    Lori L. Burrows

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  1. Lori L. Burrows
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Correspondence to Lori L. Burrows.

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Burrows, L.L. Heads or tails for type V pilus assembly. Nat Microbiol 5, 782–784 (2020). https://doi.org/10.1038/s41564-020-0732-y

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