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| | <StructureSection load='5cb7' size='340' side='right'caption='[[5cb7]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='5cb7' size='340' side='right'caption='[[5cb7]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cb7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rotavirus_(serotype_g1_/_strain_k8) Human rotavirus (serotype g1 / strain k8)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CB7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CB7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cb7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_A_K8/G1 Rotavirus A K8/G1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CB7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5cb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cb7 OCA], [http://pdbe.org/5cb7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cb7 RCSB], [http://www.ebi.ac.uk/pdbsum/5cb7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cb7 ProSAT]</span></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=5cb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cb7 OCA], [https://pdbe.org/5cb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cb7 RCSB], [https://www.ebi.ac.uk/pdbsum/5cb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cb7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VP4_ROTHJ VP4_ROTHJ]] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity). Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment (By similarity). VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact (By similarity). | + | [https://www.uniprot.org/uniprot/VP4_ROTHJ VP4_ROTHJ] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity). Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment (By similarity). VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blanchard, H]]
| + | [[Category: Rotavirus A K8/G1]] |
| - | [[Category: Yu, X]]
| + | [[Category: Blanchard H]] |
| - | [[Category: Carbohydrate-recognizing protein]]
| + | [[Category: Yu X]] |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Rotavirus]] | + | |
| - | [[Category: Sugar binding protein]] | + | |
| - | [[Category: Viral protein]] | + | |
| - | [[Category: Vp8*]]
| + | |
| Structural highlights
5cb7 is a 2 chain structure with sequence from Rotavirus A K8/G1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
VP4_ROTHJ Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity). Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment (By similarity). VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact (By similarity).
Publication Abstract from PubMed
Rotavirus-cell binding is the essential first step in rotavirus infection. This binding is a major determinant of rotavirus tropism, as host cell invasion is necessary to initiate infection. Initial rotavirus-cell interactions are mediated by carbohydrate-recognizing domain VP8* of the rotavirus capsid spike protein VP4. Here, we report the first observation of significant structural rearrangement of VP8* from human and animal rotavirus strains upon glycan receptor binding. The structural adaptability of rotavirus VP8* delivers important insights into how human and animal rotaviruses utilize the wider range of cellular glycans identified as VP8* binding partners. Furthermore, our studies on rotaviruses with atypical genetic makeup provide information expected to be critical for understanding the mechanisms of animal rotavirus gene emergence in humans and support implementation of epidemiologic surveillance of animal reservoirs as well as future vaccination schemes.
Substantial Receptor-induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross-Species Infection.,Yu X, Mishra R, Holloway G, von Itzstein M, Coulson BS, Blanchard H Chembiochem. 2015 Oct 12;16(15):2176-81. doi: 10.1002/cbic.201500360. Epub 2015, Sep 3. PMID:26250751[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu X, Mishra R, Holloway G, von Itzstein M, Coulson BS, Blanchard H. Substantial Receptor-induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross-Species Infection. Chembiochem. 2015 Oct 12;16(15):2176-81. doi: 10.1002/cbic.201500360. Epub 2015, Sep 3. PMID:26250751 doi:http://dx.doi.org/10.1002/cbic.201500360
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