View source for 8tea


==HCMV Pentamer in complex with CS2pt1p2_A10L Fab and CS3pt1p4_C1L Fab==
<StructureSection load='8tea' size='340' side='right'caption='[[8tea]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8tea]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [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=8TEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TEA 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]] 3.4&#8491;</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=8tea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tea OCA], [https://pdbe.org/8tea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tea RCSB], [https://www.ebi.ac.uk/pdbsum/8tea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tea ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q38M12_HCMV Q38M12_HCMV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human cytomegalovirus (HCMV) can cause severe diseases in fetuses, newborns, and immunocompromised individuals. Currently, no vaccines are approved, and treatment options are limited. Here, we analyzed the human B cell response of four HCMV top neutralizers from a cohort of 9,000 individuals. By single-cell analyses of memory B cells targeting the pentameric and trimeric HCMV surface complexes, we identified vulnerable sites on the shared gH/gL subunits as well as complex-specific subunits UL(128/130/131A) and gO. Using high-resolution cryogenic electron microscopy, we revealed the structural basis of the neutralization mechanisms of antibodies targeting various binding sites. Moreover, we identified highly potent antibodies that neutralized a broad spectrum of HCMV strains, including primary clinical isolates, that outperform known antibodies used in clinical trials. Our study provides a deep understanding of the mechanisms of HCMV neutralization and identifies promising antibody candidates to prevent and treat HCMV infection.

Single-cell analysis of memory B cells from top neutralizers reveals multiple sites of vulnerability within HCMV Trimer and Pentamer.,Zehner M, Alt M, Ashurov A, Goldsmith JA, Spies R, Weiler N, Lerma J, Gieselmann L, Stohr D, Gruell H, Schultz EP, Kreer C, Schlachter L, Janicki H, Laib Sampaio K, Stegmann C, Nemetchek MD, Dahling S, Ullrich L, Dittmer U, Witzke O, Koch M, Ryckman BJ, Lotfi R, McLellan JS, Krawczyk A, Sinzger C, Klein F Immunity. 2023 Nov 14;56(11):2602-2620.e10. doi: 10.1016/j.immuni.2023.10.009. PMID:37967532<ref>PMID:37967532</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8tea" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human betaherpesvirus 5]]
[[Category: Large Structures]]
[[Category: Goldsmith JA]]
[[Category: McLellan JS]]