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6gsi

From Proteopedia

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Current revision

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.

6gsi, resolution 3.75Å

Structural highlights

6gsi is a 12 chain structure with sequence from Cat and Feline calicivirus strain f9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	6gsh
Gene:	F11R, JAM1 (Cat)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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. [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). [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.^[1] ^[2] (Microbial infection) In case of orthoreovirus infection, serves as receptor for the virus.^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Makino A, Shimojima M, Miyazawa T, Kato K, Tohya Y, Akashi H. Junctional adhesion molecule 1 is a functional receptor for feline calicivirus. J Virol. 2006 May;80(9):4482-90. PMID:16611908 doi:http://dx.doi.org/80/9/4482
↑ Ossiboff RJ, Parker JS. Identification of regions and residues in feline junctional adhesion molecule required for feline calicivirus binding and infection. J Virol. 2007 Dec;81(24):13608-21. Epub 2007 Oct 3. PMID:17913818 doi:http://dx.doi.org/JVI.01509-07
↑ Barton ES, Forrest JC, Connolly JL, Chappell JD, Liu Y, Schnell FJ, Nusrat A, Parkos CA, Dermody TS. Junction adhesion molecule is a receptor for reovirus. Cell. 2001 Feb 9;104(3):441-51. PMID:11239401
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6gsi"

@@ Line 3: / Line 3: @@
 <SX load='6gsi' size='340' side='right' viewer='molstar' caption='[[6gsi]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
 == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GSI FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gsh|6gsh]]</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'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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>
 == Function ==
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 6gsi" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>

6gsi

From Proteopedia

Current revision

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.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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