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Structural basis for assembly of vertical single β-barrel viruses

Author

Listed:
  • Isaac Santos-Pérez

    (CIBERehd)

  • Diego Charro

    (CIBERehd)

  • David Gil-Carton

    (CIBERehd)

  • Mikel Azkargorta

    (ProteoRed-ISCIII)

  • Felix Elortza

    (ProteoRed-ISCIII)

  • Dennis H. Bamford

    (University of Helsinki)

  • Hanna M. Oksanen

    (University of Helsinki)

  • Nicola G. A. Abrescia

    (CIBERehd
    Basque Foundation for Science)

Abstract

The vertical double β-barrel major capsid protein (MCP) fold, fingerprint of the PRD1-adeno viral lineage, is widespread in many viruses infecting organisms across the three domains of life. The discovery of PRD1-like viruses with two MCPs challenged the known assembly principles. Here, we present the cryo-electron microscopy (cryo-EM) structures of the archaeal, halophilic, internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) and Haloarcula hispanica icosahedral virus 2 (HHIV-2) at 3.7 and 3.8 Å resolution, respectively. Our structures reveal proteins located beneath the morphologically distinct two- and three-tower capsomers and homopentameric membrane proteins at the vertices that orchestrate the positioning of pre-formed vertical single β-barrel MCP heterodimers. The cryo-EM based structures together with the proteomics data provide insights into the assembly mechanism of this type of viruses and into those with membrane-less double β-barrel MCPs.

Suggested Citation

  • Isaac Santos-Pérez & Diego Charro & David Gil-Carton & Mikel Azkargorta & Felix Elortza & Dennis H. Bamford & Hanna M. Oksanen & Nicola G. A. Abrescia, 2019. "Structural basis for assembly of vertical single β-barrel viruses," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08927-2
    DOI: 10.1038/s41467-019-08927-2
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