Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusion
about
Multiscale perspectives of virus entry via endocytosisBinding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesionMultiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infectionGlycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entryGlycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1.The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entryStructure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.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.Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface.A herpes simplex virus 2 glycoprotein D mutant generated by bacterial artificial chromosome mutagenesis is severely impaired for infecting neuronal cells and infects only Vero cells expressing exogenous HVEM.The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.An HSV-1 gD mutant virus as an entry-impaired live virus vaccine.Potential nectin-1 binding site on herpes simplex virus glycoprotein d.Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection.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 familyThe herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2.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.Rational development of beta-peptide inhibitors of human cytomegalovirus entry.
P2860
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P2860
Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusion
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Function of herpes simplex vir ...... ties in virus entry and fusion
@ast
Function of herpes simplex vir ...... ties in virus entry and fusion
@en
type
label
Function of herpes simplex vir ...... ties in virus entry and fusion
@ast
Function of herpes simplex vir ...... ties in virus entry and fusion
@en
prefLabel
Function of herpes simplex vir ...... ties in virus entry and fusion
@ast
Function of herpes simplex vir ...... ties in virus entry and fusion
@en
P2093
P2860
P1433
P1476
Function of herpes simplex vir ...... ties in virus entry and fusion
@en
P2093
Gary H Cohen
Richard S B Milne
Sharon H Willis
Sheri L Hanna
P2860
P304
P356
10.1128/JVI.77.16.8962-8972.2003
P407
P577
2003-08-01T00:00:00Z