Calicivirus VP2 forms a portal-like assembly following receptor engagement

Michaela J. Conley, Marion McElwee, Liyana Azmi, Mads Gabrielsen, Olwyn Byron, Ian G. Goodfellow and David Bhella ()
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Michaela J. Conley: Medical Research Council University of Glasgow Centre for Virus Research
Marion McElwee: Medical Research Council University of Glasgow Centre for Virus Research
Liyana Azmi: University of Glasgow
Mads Gabrielsen: CRUK Beatson Institute
Olwyn Byron: University of Glasgow
Ian G. Goodfellow: University of Cambridge
David Bhella: Medical Research Council University of Glasgow Centre for Virus Research

Nature, 2019, vol. 565, issue 7739, 377-381

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41586-018-0852-1

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