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CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae

Author

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  • Sara J. Weaver

    (California Institute of Technology
    University of California Los Angeles)

  • Davi R. Ortega

    (California Institute of Technology)

  • Matthew H. Sazinsky

    (Pomona College)

  • Triana N. Dalia

    (Indiana University)

  • Ankur B. Dalia

    (Indiana University)

  • Grant J. Jensen

    (California Institute of Technology)

Abstract

Natural transformation is the process by which bacteria take up genetic material from their environment and integrate it into their genome by homologous recombination. It represents one mode of horizontal gene transfer and contributes to the spread of traits like antibiotic resistance. In Vibrio cholerae, a type IVa pilus (T4aP) is thought to facilitate natural transformation by extending from the cell surface, binding to exogenous DNA, and retracting to thread this DNA through the outer membrane secretin, PilQ. Here, we use a functional tagged allele of VcPilQ purified from native V. cholerae cells to determine the cryoEM structure of the VcPilQ secretin in amphipol to ~2.7 Å. We use bioinformatics to examine the domain architecture and gene neighborhood of T4aP secretins in Proteobacteria in comparison with VcPilQ. This structure highlights differences in the architecture of the T4aP secretin from the type II and type III secretion system secretins. Based on our cryoEM structure, we design a series of mutants to reversibly regulate VcPilQ gate dynamics. These experiments support the idea of VcPilQ as a potential druggable target and provide insight into the channel that DNA likely traverses to promote the spread of antibiotic resistance via horizontal gene transfer by natural transformation.

Suggested Citation

  • Sara J. Weaver & Davi R. Ortega & Matthew H. Sazinsky & Triana N. Dalia & Ankur B. Dalia & Grant J. Jensen, 2020. "CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18866-y
    DOI: 10.1038/s41467-020-18866-y
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    Cited by:

    1. Sebastian A. G. Braus & Francesca L. Short & Stefanie Holz & Matthew J. M. Stedman & Alvar D. Gossert & Manuela K. Hospenthal, 2022. "The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Rebecca Conners & Mathew McLaren & Urszula Łapińska & Kelly Sanders & M. Rhia L. Stone & Mark A. T. Blaskovich & Stefano Pagliara & Bertram Daum & Jasna Rakonjac & Vicki A. M. Gold, 2021. "CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    3. Matteo Tassinari & Marta Rudzite & Alain Filloux & Harry H. Low, 2023. "Assembly mechanism of a Tad secretion system secretin-pilotin complex," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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