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| | <SX load='6gsi' size='340' side='right' viewer='molstar' caption='[[6gsi]], [[Resolution|resolution]] 3.75Å' scene=''> | | <SX load='6gsi' size='340' side='right' viewer='molstar' caption='[[6gsi]], [[Resolution|resolution]] 3.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gsi]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Cat Cat] and [http://en.wikipedia.org/wiki/Feline_calicivirus_strain_f9 Feline calicivirus strain f9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6GSI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gsi]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Feline_calicivirus_strain_F9 Feline calicivirus strain F9] and [https://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GSI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gsh|6gsh]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F11R, JAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9685 Cat])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6gsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsi OCA], [https://pdbe.org/6gsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gsi RCSB], [https://www.ebi.ac.uk/pdbsum/6gsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsi ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6gsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsi OCA], [http://pdbe.org/6gsi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gsi RCSB], [http://www.ebi.ac.uk/pdbsum/6gsi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSD_FCVF9 CAPSD_FCVF9]] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm. [[http://www.uniprot.org/uniprot/VP2_FCVF9 VP2_FCVF9]] Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). [[http://www.uniprot.org/uniprot/JAM1_FELCA JAM1_FELCA]] Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration. Involved in platelet activation.[UniProtKB:O88792][UniProtKB:Q9Y624] (Microbial infection) May act as a cellular receptor for calicivirus.<ref>PMID:16611908</ref> <ref>PMID:17913818</ref> (Microbial infection) In case of orthoreovirus infection, serves as receptor for the virus.<ref>PMID:11239401</ref> | + | [https://www.uniprot.org/uniprot/CAPSD_FCVF9 CAPSD_FCVF9] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Cat]] | + | [[Category: Feline calicivirus strain F9]] |
| - | [[Category: Feline calicivirus strain f9]] | + | [[Category: Felis catus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhella, D]] | + | [[Category: Bhella D]] |
| - | [[Category: Conley, M J]] | + | [[Category: Conley MJ]] |
| - | [[Category: Calicivirus]]
| + | |
| - | [[Category: Capsid]]
| + | |
| - | [[Category: Junctional-adhesion molecule some]]
| + | |
| - | [[Category: Portal]]
| + | |
| - | [[Category: Vesivirus]]
| + | |
| - | [[Category: Virus]]
| + | |
| - | [[Category: Vp1]]
| + | |
| - | [[Category: Vp2]]
| + | |
| Structural highlights
Function
CAPSD_FCVF9 Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm.
Publication Abstract from PubMed
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(1,2), 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(3); our findings provide insights into its structure and function that advance our understanding of the Caliciviridae.
Calicivirus VP2 forms a portal-like assembly following receptor engagement.,Conley MJ, McElwee M, Azmi L, Gabrielsen M, Byron O, Goodfellow IG, Bhella D Nature. 2019 Jan;565(7739):377-381. doi: 10.1038/s41586-018-0852-1. Epub 2019 Jan, 9. PMID:30626974[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Conley MJ, McElwee M, Azmi L, Gabrielsen M, Byron O, Goodfellow IG, Bhella D. Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature. 2019 Jan;565(7739):377-381. doi: 10.1038/s41586-018-0852-1. Epub 2019 Jan, 9. PMID:30626974 doi:http://dx.doi.org/10.1038/s41586-018-0852-1
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