Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex.
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Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusionBlocking antibody access to neutralizing domains on glycoproteins involved in entry as a novel mechanism of immune evasion by herpes simplex virus type 1 glycoproteins C and EHerpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BEmerging Vaccine TechnologiesStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryCrystal structure of the conserved herpesvirus fusion regulator complex gH–gLStructure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibodyCrystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexCharacterization of Vesicular Stomatitis Virus Pseudotypes Bearing Essential Entry Glycoproteins gB, gD, gH, and gL of Herpes Simplex Virus 1.Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1.The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Herpes virus fusion and entry: a story with many characters.Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function.Dissection of the antibody response against herpes simplex virus glycoproteins in naturally infected humansRhesus and human cytomegalovirus glycoprotein L are required for infection and cell-to-cell spread of virus but cannot complement each other.Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD.A novel function of heparan sulfate in the regulation of cell-cell fusion.Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasThe herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry.A site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex gHgL.Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry.N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for functionMutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function.Functional analysis of glycoprotein L (gL) from rhesus lymphocryptovirus in Epstein-Barr virus-mediated cell fusion indicates a direct role of gL in gB-induced membrane fusion.Insertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.Mutations in the amino terminus of herpes simplex virus type 1 gL can reduce cell-cell fusion without affecting gH/gL trafficking.Assembly and organization of glycoproteins B, C, D, and H in herpes simplex virus type 1 particles lacking individual glycoproteins: No evidence for the formation of a complex of these molecules.Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies.Heptad repeat 2 in herpes simplex virus 1 gH interacts with heptad repeat 1 and is critical for virus entry and fusion.A heptad repeat in herpes simplex virus 1 gH, located downstream of the alpha-helix with attributes of a fusion peptide, is critical for virus entry and fusion.The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae familyIntracellular processing of human herpesvirus 6 glycoproteins Q1 and Q2 into tetrameric complexes expressed on the viral envelope.Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD Is Defined by Using Alphaherpesvirus gH and gL Chimeras.Sialic acid on herpes simplex virus type 1 envelope glycoproteins is required for efficient infection of cellsEpstein-Barr virus fusion with epithelial cells triggered by gB is restricted by a gL glycosylation site.Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion.
P2860
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P2860
Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Structural and antigenic analy ...... us glycoprotein gH-gL complex.
@ast
Structural and antigenic analy ...... us glycoprotein gH-gL complex.
@en
type
label
Structural and antigenic analy ...... us glycoprotein gH-gL complex.
@ast
Structural and antigenic analy ...... us glycoprotein gH-gL complex.
@en
prefLabel
Structural and antigenic analy ...... us glycoprotein gH-gL complex.
@ast
Structural and antigenic analy ...... us glycoprotein gH-gL complex.
@en
P2093
P2860
P1433
P1476
Structural and antigenic analy ...... rus glycoprotein gH-gL complex
@en
P2093
J D Lambris
M J Novotny
M Ponce de Leon
R J Eisenberg
P2860
P304
P577
1998-07-01T00:00:00Z