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The structures of two archaeal type IV pili illuminate evolutionary relationships

Author

Listed:
  • Fengbin Wang

    (University of Virginia)

  • Diana P. Baquero

    (Archaeal Virology Unit, Department of Microbiology Institut Pasteur
    Sorbonne Universités, Collège Doctoral)

  • Zhangli Su

    (University of Virginia)

  • Leticia C. Beltran

    (University of Virginia)

  • David Prangishvili

    (Archaeal Virology Unit, Department of Microbiology Institut Pasteur
    Ivane Javakhishvili Tbilisi State University)

  • Mart Krupovic

    (Archaeal Virology Unit, Department of Microbiology Institut Pasteur)

  • Edward H. Egelman

    (University of Virginia)

Abstract

We have determined the cryo-electron microscopic (cryo-EM) structures of two archaeal type IV pili (T4P), from Pyrobaculum arsenaticum and Saccharolobus solfataricus, at 3.8 Å and 3.4 Å resolution, respectively. This triples the number of high resolution archaeal T4P structures, and allows us to pinpoint the evolutionary divergence of bacterial T4P, archaeal T4P and archaeal flagellar filaments. We suggest that extensive glycosylation previously observed in T4P of Sulfolobus islandicus is a response to an acidic environment, as at even higher temperatures in a neutral environment much less glycosylation is present for Pyrobaculum than for Sulfolobus and Saccharolobus pili. Consequently, the Pyrobaculum filaments do not display the remarkable stability of the Sulfolobus filaments in vitro. We identify the Saccharolobus and Pyrobaculum T4P as host receptors recognized by rudivirus SSRV1 and tristromavirus PFV2, respectively. Our results illuminate the evolutionary relationships among bacterial and archaeal T4P filaments and provide insights into archaeal virus-host interactions.

Suggested Citation

  • Fengbin Wang & Diana P. Baquero & Zhangli Su & Leticia C. Beltran & David Prangishvili & Mart Krupovic & Edward H. Egelman, 2020. "The structures of two archaeal type IV pili illuminate evolutionary relationships," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17268-4
    DOI: 10.1038/s41467-020-17268-4
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    Cited by:

    1. Lavinia Gambelli & Michail N. Isupov & Rebecca Conners & Mathew McLaren & Annett Bellack & Vicki Gold & Reinhard Rachel & Bertram Daum, 2022. "An archaellum filament composed of two alternating subunits," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Junfeng Liu & Gunnar N. Eastep & Virginija Cvirkaite-Krupovic & Shane T. Rich-New & Mark A. B. Kreutzberger & Edward H. Egelman & Mart Krupovic & Fengbin Wang, 2024. "Two distinct archaeal type IV pili structures formed by proteins with identical sequence," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Matthew C. Gaines & Shamphavi Sivabalasarma & Michail N. Isupov & Risat Ul Haque & Mathew McLaren & Cyril Hanus & Vicki A. M. Gold & Sonja-Verena Albers & Bertram Daum, 2024. "CryoEM reveals the structure of an archaeal pilus involved in twitching motility," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Matthew C. Gaines & Michail N. Isupov & Shamphavi Sivabalasarma & Risat Ul Haque & Mathew McLaren & Clara L. Mollat & Patrick Tripp & Alexander Neuhaus & Vicki A. M. Gold & Sonja-Verena Albers & Bertr, 2022. "Electron cryo-microscopy reveals the structure of the archaeal thread filament," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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