Functional analysis of glycoprotein L (gL) from rhesus lymphocryptovirus in Epstein-Barr virus-mediated cell fusion indicates a direct role of gL in gB-induced membrane fusion.
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Human herpesvirus 6 glycoprotein complex formation is required for folding and trafficking of the gH/gL/gQ1/gQ2 complex and its cellular receptor bindingStructural and Mechanistic Insights into the Tropism of Epstein-Barr VirusStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryCrystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexMechanism for neutralizing activity by the anti-CMV gH/gL monoclonal antibody MSL-109Assembly and architecture of the EBV B cell entry triggering complexCharacteristics of Epstein-Barr virus envelope protein gp42.Herpes virus fusion and entry: a story with many characters.The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cellsMapping regions of Epstein-Barr virus (EBV) glycoprotein B (gB) important for fusion function with gH/gL.Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.A site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex gHgL.Fusing structure and function: a structural view of the herpesvirus entry machinery.Scanning Mutagenesis of Human Cytomegalovirus Glycoprotein gH/gL.Human Cytomegalovirus gH/gL/gO Promotes the Fusion Step of Entry into All Cell Types, whereas gH/gL/UL128-131 Broadens Virus Tropism through a Distinct Mechanism.A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Epstein-Barr virus transcytosis through polarized oral epithelial cellsInsertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD Is Defined by Using Alphaherpesvirus gH and gL Chimeras.Epstein-Barr virus fusion with epithelial cells triggered by gB is restricted by a gL glycosylation site.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.A conserved Eph family receptor-binding motif on the gH/gL complex of Kaposi's sarcoma-associated herpesvirus and rhesus monkey rhadinovirus.An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus.
P2860
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P2860
Functional analysis of glycoprotein L (gL) from rhesus lymphocryptovirus in Epstein-Barr virus-mediated cell fusion indicates a direct role of gL in gB-induced 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 20 May 2009
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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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name
Functional analysis of glycopr ...... in gB-induced membrane fusion.
@en
Functional analysis of glycoprotein L
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type
label
Functional analysis of glycopr ...... in gB-induced membrane fusion.
@en
Functional analysis of glycoprotein L
@nl
prefLabel
Functional analysis of glycopr ...... in gB-induced membrane fusion.
@en
Functional analysis of glycoprotein L
@nl
P2093
P2860
P356
P1433
P1476
Functional analysis of glycopr ...... in gB-induced membrane fusion.
@en
P2093
Aileen E Plate
Jasmina Smajlović
Richard Longnecker
Theodore S Jardetzky
P2860
P304
P356
10.1128/JVI.00457-09
P407
P577
2009-05-20T00:00:00Z