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The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins

Author

Listed:
  • Kamel El Omari

    (University of Oxford
    Diamond Light Source Limited, Harwell Science and Innovation Campus)

  • Sai Li

    (University of Oxford
    School of Life Sciences, Tsinghua University)

  • Abhay Kotecha

    (University of Oxford)

  • Thomas S. Walter

    (University of Oxford)

  • Eduardo A. Bignon

    (Laboratorio de Virología Molecular)

  • Karl Harlos

    (University of Oxford)

  • Pentti Somerharju

    (University of Helsinki)

  • Felix Haas

    (Thermo Fisher Scientific)

  • Daniel K. Clare

    (Diamond Light Source Limited, Harwell Science and Innovation Campus)

  • Mika Molin

    (Institute of Biotechnology, University of Helsinki)

  • Felipe Hurtado

    (Laboratorio de Virología Molecular)

  • Mengqiu Li

    (University of Oxford)

  • Jonathan M. Grimes

    (University of Oxford
    Diamond Light Source Limited, Harwell Science and Innovation Campus)

  • Dennis H. Bamford

    (University of Helsinki)

  • Nicole D. Tischler

    (Laboratorio de Virología Molecular)

  • Juha T. Huiskonen

    (University of Oxford
    University of Helsinki)

  • David I. Stuart

    (University of Oxford
    Diamond Light Source Limited, Harwell Science and Innovation Campus)

  • Elina Roine

    (University of Helsinki)

Abstract

Lipid membrane fusion is an essential function in many biological processes. Detailed mechanisms of membrane fusion and the protein structures involved have been mainly studied in eukaryotic systems, whereas very little is known about membrane fusion in prokaryotes. Haloarchaeal pleomorphic viruses (HRPVs) have a membrane envelope decorated with spikes that are presumed to be responsible for host attachment and membrane fusion. Here we determine atomic structures of the ectodomains of the 57-kDa spike protein VP5 from two related HRPVs revealing a previously unreported V-shaped fold. By Volta phase plate cryo-electron tomography we show that VP5 is monomeric on the viral surface, and we establish the orientation of the molecules with respect to the viral membrane. We also show that the viral membrane fuses with the host cytoplasmic membrane in a process mediated by VP5. This sheds light on protein structures involved in prokaryotic membrane fusion.

Suggested Citation

  • Kamel El Omari & Sai Li & Abhay Kotecha & Thomas S. Walter & Eduardo A. Bignon & Karl Harlos & Pentti Somerharju & Felix Haas & Daniel K. Clare & Mika Molin & Felipe Hurtado & Mengqiu Li & Jonathan M., 2019. "The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08728-7
    DOI: 10.1038/s41467-019-08728-7
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    Cited by:

    1. David Moi & Shunsuke Nishio & Xiaohui Li & Clari Valansi & Mauricio Langleib & Nicolas G. Brukman & Kateryna Flyak & Christophe Dessimoz & Daniele de Sanctis & Kathryn Tunyasuvunakool & John Jumper & , 2022. "Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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