Publication: Calicivirus VP2 Forms A Portal-like Assembly Following Receptor Engagement
dc.contributor.author | Michaela J. Conley | en_US |
dc.contributor.author | Marion McElwee | en_US |
dc.contributor.author | Liyana Azmi | en_US |
dc.contributor.author | Mads Gabrielsen | en_US |
dc.contributor.author | Olwyn Byron | en_US |
dc.contributor.author | Ian G. Goodfellow | en_US |
dc.contributor.author | David Bhella | en_US |
dc.date.accessioned | 2024-05-28T03:28:36Z | |
dc.date.available | 2024-05-28T03:28:36Z | |
dc.date.issued | 2019 | |
dc.date.submitted | 18/2/2020 | |
dc.description | Conley, 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/s41586-018-0852-1 | en_US |
dc.description.abstract | To 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.doi | 10.1038/s41586-018-0852-1 | |
dc.identifier.epage | 381 | |
dc.identifier.issn | 0028-0836 | |
dc.identifier.issue | 7739 | |
dc.identifier.other | 2409-1 | |
dc.identifier.spage | 377 | |
dc.identifier.uri | https://www.nature.com/articles/s41586-018-0852-1 | |
dc.identifier.uri | https://oarep.usim.edu.my/handle/123456789/4341 | |
dc.identifier.volume | 565 | |
dc.language.iso | en | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.relation.ispartof | Nature | en_US |
dc.subject | Cryoelectron microscopy | en_US |
dc.subject | SAXS | en_US |
dc.subject | Virus–host interactions | en_US |
dc.subject | Virus structures | en_US |
dc.title | Calicivirus VP2 Forms A Portal-like Assembly Following Receptor Engagement | en_US |
dc.type | Article | en_US |
dspace.entity.type | Publication |