9dix: Difference between revisions

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'''Unreleased structure'''


The entry 9dix is ON HOLD
==HCMV gH/UL116/UL141 3-mer complex, ectodomain==
<StructureSection load='9dix' size='340' side='right'caption='[[9dix]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9dix]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DIX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.51&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=9dix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dix OCA], [https://pdbe.org/9dix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dix RCSB], [https://www.ebi.ac.uk/pdbsum/9dix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dix ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human cytomegalovirus (HCMV) causes severe birth defects, lifelong health complications, and $4 billion in annual costs in the United States alone. A major challenge in vaccine design is the incomplete understanding of the diverse protein complexes the virus uses to infect cells. In Herpesviridae, the gH/gL glycoprotein heterodimer is expected to be a basal element of virion cell entry machinery. For HCMV, gH/gL forms a "trimer" with gO and a "pentamer" with UL128, UL130, and UL131A, with each complex binding distinct receptors to enter varied cell types. Here, we reveal a third glycoprotein complex, abundant in HCMV virions, which significantly enhances infection of endothelial cells. In this "3-mer" complex, gH, without gL, associates with UL116 and UL141, an immunoevasin previously known to function in an intracellular role. Cryo-EM reveals the virion-surface 3-mer is structurally unique among Herpesviridae gH complexes, with gH-only scaffolding, UL141-mediated dimerization and a heavily glycosylated UL116 cap. Given that antibodies directed at gH and UL141 each can restrict HCMV replication, our work highlights this virion surface complex as a new target for vaccines and antiviral therapies.


Authors:  
A noncanonical glycoprotein H complex enhances cytomegalovirus entry.,Norris MJ, Henderson LA, Siddiquey MNA, Yin J, Yoo K, Brunel S, Saphire EO, Benedict CA, Kamil JP bioRxiv [Preprint]. 2024 Oct 13:2024.10.13.617647. doi: , 10.1101/2024.10.13.617647. PMID:39416215<ref>PMID:39416215</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9dix" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human betaherpesvirus 5]]
[[Category: Large Structures]]
[[Category: Benedict CA]]
[[Category: Kamil JP]]
[[Category: Norris MJ]]
[[Category: Saphire EO]]
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