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    Cryo-EM structures of two Bacteriophage portal proteins provide insights for antimicrobial phage engineering

    Javed, Abid and Villanueva, Hugo and Shataer, S. and Vasciaveo, S. and Savva, Renos and Orlova, Elena (2021) Cryo-EM structures of two Bacteriophage portal proteins provide insights for antimicrobial phage engineering. Viruses 13 (12), ISSN 1999-4915.

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    Abstract

    Widespread antibiotic resistance has returned attention to bacteriophages as a means of managing bacterial pathogenesis. Synthetic biology approaches to engineer phages have demonstrated genomic editing to broaden natural host ranges, or to optimise microbicidal action. Gram positive pathogens cause serious pastoral animal and human infections that are especially lethal in newborns. Such pathogens are targeted by the obligate lytic phages of the and families. These phages have relatively small ~20 kb linear protein-capped genomes and their compact organisation, relatively few structural elements, and broad host range, are appealing from a phage-engineering standpoint. In this study, we focus on portal proteins, which are core elements for the assembly of such tailed phages. The structures of dodecameric portal complexes from phage GA1, which targets , and phage phiCPV4 that infects , were determined at resolutions of 3.3 Å and 2.9 Å, respectively. Both are found to closely resemble the related phi29 portal protein fold. However, the portal protein of phiCPV4 exhibits interesting differences in the clip domain. These structures provide new insights on structural diversity in portal proteins and will be essential for considerations in phage structural engineering.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): portal protein, bacteriophage, clip domain, phiCPV4, structural analysis, cryo electron microscopy, GA1
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    SWORD Depositor: Mr Joe Tenant
    Depositing User: Mr Joe Tenant
    Date Deposited: 19 Jul 2022 11:43
    Last Modified: 02 Aug 2023 18:15
    URI: https://eprints.bbk.ac.uk/id/eprint/47243

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