Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion.
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Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusionHerpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BStructure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entryThe 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.Herpes virus fusion and entry: a story with many characters.Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.The nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.Molecular gymnastics at the herpesvirus surface.Herpes simplex type 2 virus deleted in glycoprotein D protects against vaginal, skin and neural disease.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.The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.Displacement of the C terminus of herpes simplex virus gD is sufficient to expose the fusion-activating interfaces on gD.Herpes simplex virus infects most cell types in vitro: clues to its successCharacterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection.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.Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry.Substitution of herpes simplex virus 1 entry glycoproteins with those of saimiriine herpesvirus 1 reveals a gD-gH/gL functional interaction and a region within the gD profusion domain that is critical for fusion.Mutations in herpes simplex virus gD protein affect receptor binding by different molecular mechanisms.
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Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 06 December 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Use of herpes simplex virus an ...... critical for membrane fusion.
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Use of herpes simplex virus an ...... critical for membrane fusion.
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Use of herpes simplex virus an ...... critical for membrane fusion.
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Use of herpes simplex virus an ...... critical for membrane fusion.
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Use of herpes simplex virus an ...... critical for membrane fusion.
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Use of herpes simplex virus an ...... critical for membrane fusion.
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Cheryl R Jogger
Patricia G Spear
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17498-17503
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10.1073/PNAS.0408186101
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2004-12-06T00:00:00Z