|Entry||Database: PDB / ID: 6gsh|
|Title||Feline Calicivirus Strain F9|
|Keywords||VIRUS / Capsid / Calicivirus / Vesivirus / Vp1|
|Function / homology||Calicivirus coat protein / Viral coat protein subunit / Picornavirus/Calicivirus coat protein / Calicivirus coat protein / Jelly Rolls - #20 / Jelly Rolls / Sandwich / Mainly Beta / VP1|
Function and homology information
|Biological species||Feline calicivirus|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å|
|Authors||Conley, M.J. / Bhella, D.|
|Funding support|| United Kingdom, 2items |
|Citation||Journal: Nature / Year: 2019|
Title: Calicivirus VP2 forms a portal-like assembly following receptor engagement.
Authors: Michaela J Conley / Marion McElwee / Liyana Azmi / Mads Gabrielsen / Olwyn Byron / Ian G Goodfellow / David Bhella /
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.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: VP1x 60
Mass: 73346.664 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Feline calicivirus / Cell (production host): Crandell Reese Feline Kidney cells
Cell line (production host): Crandell Reese Feline Kidney cells
Production host: Felis catus (domestic cat) / References: UniProt: A2T4P8
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: T=3 Icosahedral Capsid. / Type: COMPLEX / Details: T=3 Icosahedral Capsid / Entity ID: 1 / Source: RECOMBINANT|
|Molecular weight||Experimental value: NO|
|Source (natural)||Organism: Feline calicivirus|
|Source (recombinant)||Organism: Felis catus (domestic cat)|
|Details of virus||Empty: NO / Enveloped: NO / Isolate: STRAIN / Type: VIRION|
|Natural host||Organism: Felis catus|
|Virus shell||Name: Capsid / Diameter: 400 nm / Triangulation number (T number): 3|
|Buffer solution||pH: 7.2 / Details: Phosphate buffered saline|
|Specimen||Conc.: 1 mg/ml / Details: Purified enveloped virions / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 75000 X / Cs: 2.7 mm|
|Image recording||Electron dose: 63 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 5198 |
Details: Each micrograph was recorded as a movie of 50 individual fractions with a total dose of 63 e/angstrom squared
|Software||Name: PHENIX / Version: 1.13_2998: / Classification: refinement|
|Image processing||Details: Images were motion-corrected using motioncor2 Defocus estimation was performed using GCTF|
|CTF correction||Details: CTF correction was implemented through Relion / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Particle selection||Num. of particles selected: 59531 / Details: Autopicking in Relion|
|Symmetry||Point symmetry: I (icosahedral)|
|3D reconstruction||Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 41436 / Symmetry type: POINT|
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