Antigenic structure of soluble herpes simplex virus (HSV) glycoprotein D correlates with inhibition of HSV infection
about
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 DPrevention of genital herpes in a guinea pig model using a glycoprotein D-specific single chain antibody as a microbicideInhibition of herpes simplex virus gD and lymphotoxin-alpha binding to HveA by peptide antagonists.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 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.T cell intrinsic heterodimeric complexes between HVEM and BTLA determine receptivity to the surrounding microenvironment.Global 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 entryHSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.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 on structure and function of nectin-1/HveC.TNF Superfamily Networks: bidirectional and interference pathways of the herpesvirus entry mediator (TNFSF14)Nectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells.Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the tumor necrosis factor receptor superfamily and a mediator of HSV entryThe herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry.
P2860
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P2860
Antigenic structure of soluble herpes simplex virus (HSV) glycoprotein D correlates with inhibition of HSV infection
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Antigenic structure of soluble ...... th inhibition of HSV infection
@ast
Antigenic structure of soluble ...... th inhibition of HSV infection
@en
type
label
Antigenic structure of soluble ...... th inhibition of HSV infection
@ast
Antigenic structure of soluble ...... th inhibition of HSV infection
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prefLabel
Antigenic structure of soluble ...... th inhibition of HSV infection
@ast
Antigenic structure of soluble ...... th inhibition of HSV infection
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P2093
P2860
P1433
P1476
Antigenic structure of soluble ...... th inhibition of HSV infection
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P2093
P2860
P304
P407
P577
1997-04-01T00:00:00Z