6vlk

<table><tr><td colspan='2'>[[6vlk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_3_strain_Oka_vaccine Human herpesvirus 3 strain Oka vaccine]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VLK FirstGlance]. <br>

== Function ==

[https://www.uniprot.org/uniprot/GB_VZVO GB_VZVO] Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.[HAMAP-Rule:MF_04032]

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== Publication Abstract from PubMed ==

Members of the Herpesviridae, including the medically important alphaherpesvirus varicella-zoster virus (VZV), induce fusion of the virion envelope with cell membranes during entry, and between cells to form polykaryocytes in infected tissues. The conserved glycoproteins, gB, gH and gL, are the core functional proteins of the herpesvirus fusion complex. gB serves as the primary fusogen via its fusion loops, but functions for the remaining gB domains remain unexplained. As a pathway for biological discovery of domain function, our approach used structure-based analysis of the viral fusogen together with a neutralizing antibody. We report here a 2.8 A cryogenic-electron microscopy structure of native gB recovered from VZV-infected cells, in complex with a human monoclonal antibody, 93k. This high-resolution structure guided targeted mutagenesis at the gB-93k interface, providing compelling evidence that a domain spatially distant from the gB fusion loops is critical for herpesvirus fusion, revealing a potential new target for antiviral therapies.

A glycoprotein B-neutralizing antibody structure at 2.8 A uncovers a critical domain for herpesvirus fusion initiation.,Oliver SL, Xing Y, Chen DH, Roh SH, Pintilie GD, Bushnell DA, Sommer MH, Yang E, Carfi A, Chiu W, Arvin AM Nat Commun. 2020 Aug 18;11(1):4141. doi: 10.1038/s41467-020-17911-0. PMID:32811830<ref>PMID:32811830</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human herpesvirus 3 strain Oka vaccine]]