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 family
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PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein BHerpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BRandom linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein BCrystal structure of the conserved herpesvirus fusion regulator complex gH–gLReevaluating herpes simplex virus hemifusion.Anti-glycoprotein H antibody impairs the pathogenicity of varicella-zoster virus in skin xenografts in the SCID mouse model.Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry.Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.Characterization of the subcellular localization of herpes simplex virus type 1 proteins in living cells.Low pH-induced conformational change in herpes simplex virus glycoprotein B.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.Mutations of Epstein-Barr virus gH that are differentially able to support fusion with B cells or epithelial cells.Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function.A 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.Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD.Structural characteristics and antiviral activity of multiple peptides derived from MDV glycoproteins B and HThe herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry.Molecular gymnastics at the herpesvirus surface.Fusing structure and function: a structural view of the herpesvirus entry machinery.Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry.Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane.N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for functionPoint mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion.Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that mediates entry into epithelial and endothelial cells.Amphipathic DNA polymers exhibit antiherpetic activity in vitro and in vivo.Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB.Insertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.Amphipathic DNA polymers exhibit antiviral activity against systemic murine Cytomegalovirus infection.Mutations in the amino terminus of herpes simplex virus type 1 gL can reduce cell-cell fusion without affecting gH/gL trafficking.Peptide inhibitors against herpes simplex virus infections.Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Novel mutations in gB and gH circumvent the requirement for known gD Receptors in herpes simplex virus 1 entry and cell-to-cell spread.Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein.Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection.Phosphorothioate oligonucleotides inhibit human immunodeficiency virus type 1 fusion by blocking gp41 core formation.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 presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.
P2860
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P2860
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 family
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
The ectodomain of herpes simpl ...... ed in the herpesviridae family
@en
type
label
The ectodomain of herpes simpl ...... ed in the herpesviridae family
@en
prefLabel
The ectodomain of herpes simpl ...... ed in the herpesviridae family
@en
P2860
P1433
P1476
The ectodomain of herpes simpl ...... ed in the herpesviridae family
@en
P2093
Pier Luigi Martelli
Tatiana Gianni
P2860
P304
P356
10.1128/JVI.79.5.2931-2940.2005
P407
P577
2005-03-01T00:00:00Z