Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
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Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesionStructural basis for the antibody neutralization ofHerpes simplex virusGlycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entryGlobal sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.Glycoprotein D of bovine herpesvirus 5 (BoHV-5) confers an extended host range to BoHV-1 but does not contribute to invasion of the brainThe pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.Herpes simplex virus type 2 glycoprotein H interacts with integrin αvβ3 to facilitate viral entry and calcium signaling in human genital tract epithelial cells.Herpes simplex virus type 1 glycoprotein e is required for axonal localization of capsid, tegument, and membrane glycoproteins.Herpes virus fusion and entry: a story with many characters.Herpes simplex virus glycoprotein D interferes with binding of herpesvirus entry mediator to its ligands through downregulation and direct competitionStructure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.HSV activates Akt to trigger calcium release and promote viral entry: novel candidate target for treatment and suppression.Construction and properties of a herpes simplex virus 1 designed to enter cells solely via the IL-13alpha2 receptorA herpes simplex virus recombinant that exhibits a single-chain antibody to HER2/neu enters cells through the mammary tumor receptor, independently of the gD receptors.HIV-associated disruption of tight and adherens junctions of oral epithelial cells facilitates HSV-1 infection and spread.Impenetrable barriers or entry portals? The role of cell-cell adhesion during infectionFusing structure and function: a structural view of the herpesvirus entry machinery.Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins.Herpes B virus utilizes human nectin-1 but not HVEM or PILRα for cell-cell fusion and virus entry.The amino terminus of varicella-zoster virus (VZV) glycoprotein E is required for binding to insulin-degrading enzyme, a VZV receptor.Herpesvirus entry mediator on radiation-resistant cell lineages promotes ocular herpes simplex virus 1 pathogenesis in an entry-independent manner.A herpes simplex virus 2 glycoprotein D mutant generated by bacterial artificial chromosome mutagenesis is severely impaired for infecting neuronal cells and infects only Vero cells expressing exogenous HVEM.A Herpes Simplex Virus 2 (HSV-2) gD Mutant Impaired for Neural Tropism Is Superior to an HSV-2 gD Subunit Vaccine To Protect Animals from Challenge with HSV-2.Effective treatment of an orthotopic xenograft model of human glioblastoma using an EGFR-retargeted oncolytic herpes simplex virusMutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function.The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.An HSV-1 gD mutant virus as an entry-impaired live virus vaccine.Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1Rethinking herpes simplex virus: the way to oncolytic agents.Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts.Initial Contact: The First Steps in Herpesvirus Entry.Generation of herpesvirus entry mediator (HVEM)-restricted herpes simplex virus type 1 mutant viruses: resistance of HVEM-expressing cells and identification of mutations that rescue nectin-1 recognitionConstruction of a fully retargeted herpes simplex virus 1 recombinant capable of entering cells solely via human epidermal growth factor receptor 2.Herpes simplex virus Membrane Fusion.Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection.A double mutation in glycoprotein gB compensates for ineffective gD-dependent initiation of herpes simplex virus type 1 infection.Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry.Substitution of herpes simplex virus 1 entry glycoproteins with those of saimiriine herpesvirus 1 reveals a gD-gH/gL functional interaction and a region within the gD profusion domain that is critical for fusion.Mutations in herpes simplex virus gD protein affect receptor binding by different molecular mechanisms.
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P2860
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2005
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vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@en
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@nl
type
label
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@en
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@nl
prefLabel
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@en
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@nl
P2093
P2860
P1433
P1476
Potential nectin-1 binding site on herpes simplex virus glycoprotein d.
@en
P2093
Andrea Carfi
Daniel J Landsburg
Don C Wiley
Gary H Cohen
J Charles Whitbeck
Sarah A Connolly
P2860
P304
P356
10.1128/JVI.79.2.1282-1295.2005
P407
P577
2005-01-01T00:00:00Z