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| Title | Calicivirus VP2 forms a portal-like assembly following receptor engagement. |
|---|---|
| Journal, issue, pages | Nature, Vol. 565, Issue 7739, Page 377-381, Year 2019 |
| Publish date | Jan 9, 2019 |
 Authors | Michaela J Conley / Marion McElwee / Liyana Azmi / Mads Gabrielsen / Olwyn Byron / Ian G Goodfellow / David Bhella /  |
| PubMed 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 ...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, 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 virus; our findings provide insights into its structure and function that advance our understanding of the Caliciviridae. |
 External links | Nature / PubMed:30626974 |
| Methods | EM (single particle) |
| Resolution | 3.0 - 3.75 Å |
| Structure data | |
| Chemicals |  ChemComp-K: |
| Source |
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 Keywords | VIRUS / Capsid / Calicivirus / Vesivirus / Vp1 / portal / Vp2 / junctional-adhesion molecule A |
feline calicivirus
felis catus (domestic cat)
