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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.
Not available
S-EPMC1112143
|
biostudies-literature
Cite
Coexpression 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.
Not available
S-EPMC446093
|
biostudies-literature
Cite
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.
Not available
S-EPMC548475
|
biostudies-literature
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Substitution in the murine nectin1 receptor of a single conserved amino acid at a position distal from the herpes simplex virus gD binding site confers high-affinity binding to gD.
Not available
S-EPMC137010
|
biostudies-literature
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The Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its Receptors.
Not available
S-EPMC4440635
|
biostudies-literature
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{alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2.
Not available
S-EPMC3009828
|
biostudies-literature
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Replicative conditioning of Herpes simplex type 1 virus by Survivin promoter, combined to ERBB2 retargeting, improves tumour cell-restricted oncolysis.
Not available
S-EPMC7062820
|
biostudies-literature
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Preclinical therapy of disseminated HER-2⁺ ovarian and breast carcinomas with a HER-2-retargeted oncolytic herpesvirus.
Not available
S-EPMC3561254
|
biostudies-literature
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Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.
Not available
S-EPMC5411103
|
biostudies-literature
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Construction of a fully retargeted herpes simplex virus 1 recombinant capable of entering cells solely via human epidermal growth factor receptor 2.
Not available
S-EPMC2566291
|
biostudies-literature
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