Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
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A live-attenuated HSV-2 ICP0 virus elicits 10 to 100 times greater protection against genital herpes than a glycoprotein D subunit vaccineHerpes simplex virus 2 ICP0 mutant viruses are avirulent and immunogenic: implications for a genital herpes vaccineCellular localization of nectin-1 and glycoprotein D during herpes simplex virus infectionThe ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cellsCell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB)Evolutionarily divergent herpesviruses modulate T cell activation by targeting the herpesvirus entry mediator cosignaling pathwayStructure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein DSpecific association of glycoprotein B with lipid rafts during herpes simplex virus entryPrevention of genital herpes in a guinea pig model using a glycoprotein D-specific single chain antibody as a microbicideAbalone Hemocyanin Blocks the Entry of Herpes Simplex Virus 1 into Cells: a Potential New Antiviral StrategyVaccinia virus L1 binds to cell surfaces and blocks virus entry independently of glycosaminoglycansInhibition of herpes simplex virus gD and lymphotoxin-alpha binding to HveA by peptide antagonists.In vivo modulation of vaccine-induced immune responses toward a Th1 phenotype increases potency and vaccine effectiveness in a herpes simplex virus type 2 mouse model.Three-dimensional structure of herpes simplex virus type 1 glycoprotein D at 2.4-nanometer resolutionThe gH-gL complex of herpes simplex virus (HSV) stimulates neutralizing antibody and protects mice against HSV type 1 challengeMonoclonal antibodies to distinct sites on herpes simplex virus (HSV) glycoprotein D block HSV binding to HVEMHerpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry.Functional region IV of glycoprotein D from herpes simplex virus modulates glycoprotein binding to the herpesvirus entry mediatorExamination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonanceThe first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.The major neutralizing antigenic site on herpes simplex virus glycoprotein D overlaps a receptor-binding domain.Localization of the gD-binding region of the human herpes simplex virus receptor, HveAGlobal sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entryEnzymatic redesigning of biologically active heparan sulfate.Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.Herpes simplex virus glycoprotein D interferes with binding of herpesvirus entry mediator to its ligands through downregulation and direct competitionPan-HSV-2 IgG antibody in vaccinated mice and guinea pigs correlates with protection against herpes simplex virus 2.Dissection of the antibody response against herpes simplex virus glycoproteins in naturally infected humansCrystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Mucosal administration of CpG oligodeoxynucleotide elicits strong CC and CXC chemokine responses in the vagina and serves as a potent Th1-tilting adjuvant for recombinant gD2 protein vaccination against genital herpesThe 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 nectin1Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasStructure-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 fusionLow-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity.The murine homolog of human Nectin1delta serves as a species nonspecific mediator for entry of human and animal alpha herpesviruses in a pathway independent of a detectable binding to gDIdentification of novel immunodominant CD4+ Th1-type T-cell peptide epitopes from herpes simplex virus glycoprotein D that confer protective immunity.Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, nectin-2, and 3-O-sulfated heparan sulfate but not with nectin-1.
P2860
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P2860
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@ast
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@en
type
label
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@ast
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@en
prefLabel
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@ast
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@en
P2093
P2860
P1433
P1476
Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.
@en
P2093
A V Nicola
N N Naidoo
R J Eisenberg
S H Willis
P2860
P304
P407
P577
1996-06-01T00:00:00Z