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.
Summary for 6GSI
| Entry DOI | 10.2210/pdb6gsi/pdb |
| Related | 6GSH |
| EMDB information | 0054 0056 |
| Descriptor | Capsid protein, Junctional adhesion molecule A, VP2, ... (4 entities in total) |
| Functional Keywords | capsid, calicivirus, vesivirus, vp1, portal, vp2, junctional-adhesion molecule a, virus |
| Biological source | Felis catus (Domestic cat) More |
| Total number of polymer chains | 12 |
| Total formula weight | 431105.00 |
| Authors | Conley, M.J.,Bhella, D. (deposition date: 2018-06-14, release date: 2019-01-16, Last modification date: 2024-10-23) |
| Primary citation | Conley, M.J.,McElwee, M.,Azmi, L.,Gabrielsen, M.,Byron, O.,Goodfellow, I.G.,Bhella, D. Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature, 565:377-381, 2019 Cited by 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 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. PubMed: 30626974DOI: 10.1038/s41586-018-0852-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.75 Å) |
Structure validation
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