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Calicivirus VP2 Forms A Portal-like Assembly Following Receptor Engagement

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dc.contributor.authorMichaela J. Conleyen_US
dc.contributor.authorMarion McElweeen_US
dc.contributor.authorLiyana Azmien_US
dc.contributor.authorMads Gabrielsenen_US
dc.contributor.authorOlwyn Byronen_US
dc.contributor.authorIan G. Goodfellowen_US
dc.contributor.authorDavid Bhellaen_US
dc.date.accessioned2024-05-28T03:28:36Z
dc.date.available2024-05-28T03:28:36Z
dc.date.issued2019
dc.date.submitted18/2/2020
dc.descriptionConley, M.J., McElwee, M., Azmi, L. et al. Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature 565, 377–381 (2019). https://doi.org/10.1038/s41586-018-0852-1en_US
dc.description.abstractTo initiate infection, many viruses enter their host cells by triggering endocytosis following receptor engagement. However, the mechanisms by which non-enveloped viruses escape the endosome are poorly understood. Here we present near-atomic-resolution cryo-electron microscopy structures for feline calicivirus both undecorated and labelled with a soluble fragment of its cellular receptor, feline junctional adhesion molecule A. We show that VP2, a minor capsid protein encoded by all caliciviruses1,2, forms a large portal-like assembly at a unique three-fold axis of symmetry, following receptor engagement. This assembly—which was not detected in undecorated virions—is formed of twelve copies of VP2, arranged with their hydrophobic N termini pointing away from the virion surface. Local rearrangement at the portal site leads to the opening of a pore in the capsid shell. We hypothesize that the portal-like assembly functions as a channel for the delivery of the calicivirus genome, through the endosomal membrane, into the cytoplasm of a host cell, thereby initiating infection. VP2 was previously known to be critical for the production of infectious virus3; our findings provide insights into its structure and function that advance our understanding of the Caliciviridae.en_US
dc.identifier.doi10.1038/s41586-018-0852-1
dc.identifier.epage381
dc.identifier.issn0028-0836
dc.identifier.issue7739
dc.identifier.other2409-1
dc.identifier.spage377
dc.identifier.urihttps://www.nature.com/articles/s41586-018-0852-1
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/4341
dc.identifier.volume565
dc.language.isoenen_US
dc.publisherNature Publishing Groupen_US
dc.relation.ispartofNatureen_US
dc.subjectCryoelectron microscopyen_US
dc.subjectSAXSen_US
dc.subjectVirus–host interactionsen_US
dc.subjectVirus structuresen_US
dc.titleCalicivirus VP2 Forms A Portal-like Assembly Following Receptor Engagementen_US
dc.typeArticleen_US
dspace.entity.typePublication

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