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TitleCalicivirus VP2 forms a portal-like assembly following receptor engagement.
Journal, issue, pagesNature, Vol. 565, Issue 7739, Page 377-381, Year 2019
Publish dateJan 9, 2019
AuthorsMichaela J Conley / Marion McElwee / Liyana Azmi / Mads Gabrielsen / Olwyn Byron / Ian G Goodfellow / David Bhella /
PubMed AbstractTo 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 linksNature / PubMed:30626974
MethodsEM (single particle)
Resolution3.0 - 3.75 Å
Structure data

0054

6gsh

EMDB-0054, PDB-6gsh:
Feline Calicivirus Strain F9
Method: EM (single particle) / Resolution: 3.0 Å

0056

6gsi

EMDB-0056, PDB-6gsi:
Feline Calicivirus Strain F9 bound to a soluble ectodomain fragment of feline junctional adhesion molecule A - leading to assembly of a portal structure at a unique three-fold axis.
Method: EM (single particle) / Resolution: 3.75 Å

Chemicals

ChemComp-K:
Unknown entry

Source
  • feline calicivirus
  • felis catus (domestic cat)
  • feline calicivirus strain f9
KeywordsVIRUS / Capsid / Calicivirus / Vesivirus / Vp1 / portal / Vp2 / junctional-adhesion molecule A

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