7a56
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7a56]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_Schmallenberg_virus_BH80/Germany/2011 Bovine Schmallenberg virus BH80/Germany/2011]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A56 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7a56]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_Schmallenberg_virus_BH80/Germany/2011 Bovine Schmallenberg virus BH80/Germany/2011]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A56 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.85Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a56 OCA], [https://pdbe.org/7a56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a56 RCSB], [https://www.ebi.ac.uk/pdbsum/7a56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a56 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=7a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a56 OCA], [https://pdbe.org/7a56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a56 RCSB], [https://www.ebi.ac.uk/pdbsum/7a56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a56 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/GP_SBVBH GP_SBVBH] Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirus genus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc ( approximately 1,000 residues), has a variable N-terminal half (Gc(S)) targeted by the patients' antibody response and a conserved C-terminal moiety (Gc(F)) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus Gc(F), revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the Gc(S)-Gc(F) junction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines. | La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirus genus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc ( approximately 1,000 residues), has a variable N-terminal half (Gc(S)) targeted by the patients' antibody response and a conserved C-terminal moiety (Gc(F)) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus Gc(F), revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the Gc(S)-Gc(F) junction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines. | ||
| - | Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein.,Hellert J, Aebischer A, Haouz A, Guardado-Calvo P, Reiche S, Beer M, Rey FA Cell Rep. 2023 | + | Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein.,Hellert J, Aebischer A, Haouz A, Guardado-Calvo P, Reiche S, Beer M, Rey FA Cell Rep. 2023 Mar 28;42(3):112142. doi: 10.1016/j.celrep.2023.112142. Epub 2023 , Feb 22. PMID:36827185<ref>PMID:36827185</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Schmallenberg Virus Envelope Glycoprotein Gc Fusion Domains in Postfusion Conformation
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