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  1. Home
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  4. Calicivirus VP2 Forms A Portal-like Assembly Following Receptor Engagement
 
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Calicivirus VP2 Forms A Portal-like Assembly Following Receptor Engagement

Journal
Nature
Date Issued
2019
Author(s)
Michaela J. Conley
Marion McElwee
Liyana Azmi
Mads Gabrielsen
Olwyn Byron
Ian G. Goodfellow
David Bhella
DOI
10.1038/s41586-018-0852-1
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.
Subjects

Cryoelectron microsco...

SAXS

Virus–host interactio...

Virus structures

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