Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL.
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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 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.The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entryThe herpes simplex virus type 1 UL20 protein and the amino terminus of glycoprotein K (gK) physically interact with gB.Herpes simplex virus glycoproteins gH/gL and gB bind Toll-like receptor 2, and soluble gH/gL is sufficient to activate NF-κBA herpes simplex virus recombinant that exhibits a single-chain antibody to HER2/neu enters cells through the mammary tumor receptor, independently of the gD receptors.αvβ6- and αvβ8-integrins serve as interchangeable receptors for HSV gH/gL to promote endocytosis and activation of membrane fusion.The herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry.Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry.Functional and physical interactions of the herpes simplex virus type 1 UL20 membrane protein with glycoprotein KThe U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cellsThe amino terminus of herpes simplex virus type 1 glycoprotein K (gK) modulates gB-mediated virus-induced cell fusion and virion egress.The herpes simplex virus type 1 UL20 protein modulates membrane fusion events during cytoplasmic virion morphogenesis and virus-induced cell fusion.Herpes simplex virus type 1 gK is required for gB-mediated virus-induced cell fusion, while neither gB and gK nor gB and UL20p function redundantly in virion de-envelopmentGenomic Signature of the Natural Oncolytic Herpes Simplex Virus HF10 and Its Therapeutic Role in Preclinical and Clinical Trials.Syncytial Mutations Do Not Impair the Specificity of Entry and Spread of a Glycoprotein D Receptor-Retargeted Herpes Simplex Virus.Functional hierarchy of herpes simplex virus 1 viral glycoproteins in cytoplasmic virion envelopment and egressCysteines and N-glycosylation Sites Conserved Among all Alphaherpesviruses Regulate Membrane Fusion in Herpes Simplex Virus Type 1 Infection.Herpes simplex virus Membrane Fusion.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 familyCoexpression of UL20p and gK inhibits cell-cell fusion mediated by herpes simplex virus glycoproteins gD, gH-gL, and wild-type gB or an endocytosis-defective gB mutant and downmodulates their cell surface expression.The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2.Regulation of varicella-zoster virus-induced cell-to-cell fusion by the endocytosis-competent glycoproteins gH and gE.Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion.Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain.The HSV-1 mechanisms of cell-to-cell spread and fusion are critically dependent on host PTP1B.
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P2860
Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@en
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@nl
type
label
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@en
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@nl
prefLabel
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@en
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@nl
P2860
P1433
P1476
Herpes simplex virus glycoprot ...... oproteins, gD, gB, gH, and gL.
@en
P2093
Elisa Avitabile
P2860
P304
P356
10.1128/JVI.77.12.6836-6844.2003
P407
P577
2003-06-01T00:00:00Z