The major neutralizing antigenic site on herpes simplex virus glycoprotein D overlaps a receptor-binding domain.
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Antibody Recognition and Neutralization Determinants on Domains I and II of West Nile Virus Envelope ProteinStructure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1Structural basis for the antibody neutralization ofHerpes simplex virusStriking similarity of murine nectin-1alpha to human nectin-1alpha (HveC) in sequence and activity as a glycoprotein D receptor for alphaherpesvirus entry.Anti-glycoprotein H antibody impairs the pathogenicity of varicella-zoster virus in skin xenografts in the SCID mouse model.Localization of a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies.Global sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.The 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.Repertoire of epitopes recognized by serum IgG from humans vaccinated with herpes simplex virus 2 glycoprotein DThe soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entryRecent progress in herpes simplex virus immunobiology and vaccine researchAntibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.Herpes virus fusion and entry: a story with many characters.Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.Rapid progression to simian AIDS can be accompanied by selection of CD4-independent gp120 variants with impaired ability to bind CD4.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 humansBimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1Effects of herpes simplex virus type 2 glycoprotein vaccines and CLDC adjuvant on genital herpes infection in the guinea pig.Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface.Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusionB Virus (Macacine herpesvirus 1) Glycoprotein D Is Functional but Dispensable for Virus Entry into Macaque and Human Skin CellsPatient-Specific Neutralizing Antibody Responses to Herpes Simplex Virus Are Attributed to Epitopes on gD, gB, or Both and Can Be Type Specific.Using a split luciferase assay (SLA) to measure the kinetics of cell-cell fusion mediated by herpes simplex virus glycoproteins.Glycoprotein targeted therapeutics: a new era of anti-herpes simplex virus-1 therapeuticsA sugar binding protein cyanovirin-N blocks herpes simplex virus type-1 entry and cell fusion.Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism.Nasal Immunization Confers High Avidity Neutralizing Antibody Response and Immunity to Primary and Recurrent Genital Herpes in Guinea Pigs.Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion.Potential nectin-1 binding site on herpes simplex virus glycoprotein d.Herpes simplex virus infects most cell types in vitro: clues to its successThe rationale of vectored gene-fusion vaccines against cancer: evolving strategies and latest evidence.Mutations in herpes simplex virus glycoprotein D distinguish entry of free virus from cell-cell spread.Chimeric nectin1-poliovirus receptor molecules identify a nectin1 region functional in herpes simplex virus entry.Substitution in the murine nectin1 receptor of a single conserved amino acid at a position distal from the herpes simplex virus gD binding site confers high-affinity binding to gD.Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry.In vitro antiviral activity of neem (Azardirachta indica L.) bark extract against herpes simplex virus type-1 infection.
P2860
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P2860
The major neutralizing antigenic site on herpes simplex virus glycoprotein D overlaps a receptor-binding domain.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The major neutralizing antigen ...... aps a receptor-binding domain.
@ast
The major neutralizing antigen ...... aps a receptor-binding domain.
@en
type
label
The major neutralizing antigen ...... aps a receptor-binding domain.
@ast
The major neutralizing antigen ...... aps a receptor-binding domain.
@en
prefLabel
The major neutralizing antigen ...... aps a receptor-binding domain.
@ast
The major neutralizing antigen ...... aps a receptor-binding domain.
@en
P2093
P2860
P1433
P1476
The major neutralizing antigen ...... laps a receptor-binding domain
@en
P2093
A van Geelen
C Krummenacher
J C Whitbeck
M I Muggeridge
R J Eisenberg
P2860
P304
P577
1999-12-01T00:00:00Z