Calicivirus VP2 forms a portal to mediate endosome escape
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ABSTRACT:
SUBMITTER: david bhella
PROVIDER: EMPIAR-10192 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Calicivirus VP2 forms a portal-like assembly following receptor engagement.
Conley Michaela J MJ McElwee Marion M Azmi Liyana L Gabrielsen Mads M Byron Olwyn O Goodfellow Ian G IG Bhella David D
Nature 20190109 7739
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 caliciviruses ...[more]
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Project description:Feline calicivirus Genome sequencing and assembly
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