|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4d6w' size='340' side='right'caption='[[4d6w]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='4d6w' size='340' side='right'caption='[[4d6w]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d6w]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chp Chp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D6W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d6w]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chandipura_virus Chandipura virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D6W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6Å</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=4d6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6w OCA], [http://pdbe.org/4d6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d6w RCSB], [http://www.ebi.ac.uk/pdbsum/4d6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6w ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4d6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6w OCA], [https://pdbe.org/4d6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d6w RCSB], [https://www.ebi.ac.uk/pdbsum/4d6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLYCO_CHAV GLYCO_CHAV]] Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity). | + | [https://www.uniprot.org/uniprot/GLYCO_CHAV GLYCO_CHAV] Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chp]] | + | [[Category: Chandipura virus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Albertini, A]] | + | [[Category: Albertini A]] |
| - | [[Category: Baquero, E]] | + | [[Category: Baquero E]] |
| - | [[Category: Bressanelli, S]] | + | [[Category: Bressanelli S]] |
| - | [[Category: Gaudin, Y]] | + | [[Category: Gaudin Y]] |
| - | [[Category: Raux, H]] | + | [[Category: Raux H]] |
| - | [[Category: Membrane fusion]]
| + | |
| - | [[Category: Rhabdovirus]]
| + | |
| - | [[Category: Viral entry]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
GLYCO_CHAV Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity).
Publication Abstract from PubMed
Chandipura virus (CHAV), a member of the vesiculovirus genus, is an emerging human pathogen. As for other rhabdoviruses, CHAV entry into susceptible cells is mediated by its single envelope glycoprotein G which is both involved in receptor recognition and fusion of viral and cellular membranes. Here, we have characterized the fusion properties of CHAV-G. As for vesicular stomatitis virus (VSV, the prototype of the genus) G, fusion is triggered at low pH below 6.5. We have also analyzed the biochemical properties of a soluble form of CHAV-G ectodomain (CHAV-Gth, generated by thermolysin limited-proteolysis of recombinant VSV particles in which the G gene was replaced by that of CHAV). The overall behavior of CHAV-Gth is similar to that previously reported for VSV-Gth. Particularly, CHAV-Gth pre-fusion trimer is not stable in solution and low-pH-induced membrane association of CHAV-Gth is reversible. Furthermore, CHAV-Gth was crystallized in its low pH post-fusion conformation and its structure was determined at 3.6A resolution. An overall comparison of this structure with the previously reported VSV-Gth post-fusion conformation, shows a high structural similarity as expected from the comparison of primary structure. Among the three domains of G, the pleckstrin homology domain (PHD) appears to be the most divergent and the largest differences are confined to the secondary structure of the major antigenic site of rhabdoviruses. Finally, local differences indicate that CHAV has evolved alternate structural solutions in hinge regions between PH and fusion domains but also distinct pH sensitive switches. Globally the comparison between the post fusion conformation of CHAV and VSV-G highlights several features essential for the protein's function. It also reveals the remarkable plasticity of G in terms of local structures.
Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein.,Baquero E, Albertini AA, Raux H, Buonocore L, Rose JK, Bressanelli S, Gaudin Y PLoS Pathog. 2015 Mar 24;11(3):e1004756. doi: 10.1371/journal.ppat.1004756., eCollection 2015 Mar. PMID:25803715[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baquero E, Albertini AA, Raux H, Buonocore L, Rose JK, Bressanelli S, Gaudin Y. Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein. PLoS Pathog. 2015 Mar 24;11(3):e1004756. doi: 10.1371/journal.ppat.1004756., eCollection 2015 Mar. PMID:25803715 doi:http://dx.doi.org/10.1371/journal.ppat.1004756
|
