Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells.
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Cellular 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)Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deletedThe 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 DDisulfide bond structure of glycoprotein D of herpes simplex virus types 1 and 2Vaccinia virus L1 binds to cell surfaces and blocks virus entry independently of glycosaminoglycansHouttuynia cordata targets the beginning stage of herpes simplex virus infectionIdentification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis.Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infectionThe 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 gD and virions accumulate in endosomes by mannose 6-phosphate-dependent and -independent mechanisms.Herpes 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 mediatorCell surface proteoglycans are necessary for A27L protein-mediated cell fusion: identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain.The herpes simplex virus gE-gI complex facilitates cell-to-cell spread and binds to components of cell junctionsExamination 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 a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies.Herpes simplex virus with highly reduced gD levels can efficiently enter and spread between human keratinocytes.Soluble glycoprotein D blocks herpes simplex virus type 1 infection of rat eyes.Identification and characterization of a novel herpes simplex virus glycoprotein, gK, involved in cell fusionThe extracellular domain of herpes simplex virus gE is indispensable for efficient cell-to-cell spread: evidence for gE/gI receptorsHerpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entryInfection of cells by varicella zoster virus: inhibition of viral entry by mannose 6-phosphate and heparin.Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Virus receptors: implications for pathogenesis and the design of antiviral agents.Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity.Mapping of herpes simplex virus 1 genes with mutations which overcome host restrictions to infectionThe 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 gDSequential isolation of proteoglycan synthesis mutants by using herpes simplex virus as a selective agent: evidence for a proteoglycan-independent virus entry pathway.Role of mannose-6-phosphate receptors in herpes simplex virus entry into cells and cell-to-cell transmission.Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface moleculesCharacterization of cell-binding properties of bovine herpesvirus 1 glycoproteins B, C, and D: identification of a dual cell-binding function of gB.Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.Specificity and affinity of binding of herpes simplex virus type 2 glycoprotein B to glycosaminoglycans.Antigenic structure of soluble herpes simplex virus (HSV) glycoprotein D correlates with inhibition of HSV infectionCharacterization of a BHK(TK-) cell clone resistant to postattachment entry by herpes simplex virus types 1 and 2
P2860
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P2860
Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@ast
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@en
type
label
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@ast
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@en
prefLabel
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@ast
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@en
P2093
P2860
P1433
P1476
Soluble forms of herpes simple ...... nhibit virus entry into cells.
@en
P2093
P2860
P304
P407
P577
1990-06-01T00:00:00Z