Glycoprotein gL-independent infectivity of pseudorabies virus is mediated by a gD-gH fusion protein
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Egress of alphaherpesviruses: comparative ultrastructural studyRetargeting Strategies for Oncolytic Herpes Simplex VirusesTargeting of pseudorabies virus structural proteins to axons requires association of the viral Us9 protein with lipid raftsStructure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibodyCrystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexRole of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions.Glycoprotein D-independent infectivity of pseudorabies virus results in an alteration of in vivo host range and correlates with mutations in glycoproteins B and H.The absence of glycoprotein gL, but not gC or gK, severely impairs pseudorabies virus neuroinvasivenessThe UL7 gene of pseudorabies virus encodes a nonessential structural protein which is involved in virion formation and egress.Glycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H.Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasStructural and biochemical studies of HCMV gH/gL/gO and Pentamer reveal mutually exclusive cell entry complexes.Molecular gymnastics at the herpesvirus surface.The Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its ReceptorsBovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry.N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for functionFunctional Relevance of the N-Terminal Domain of Pseudorabies Virus Envelope Glycoprotein H and Its Interaction with Glycoprotein L.Mutations in Pseudorabies Virus Glycoproteins gB, gD, and gH Functionally Compensate for the Absence of gL.Comparative Mutagenesis of Pseudorabies Virus and Epstein-Barr Virus gH Identifies a Structural Determinant within Domain III of gH Required for Surface Expression and Entry FunctionFunctional Characterization of Glycoprotein H Chimeras Composed of Conserved Domains of the Pseudorabies Virus and Herpes Simplex Virus 1 Homologs.Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.The highly conserved proline at position 438 in pseudorabies virus gH is important for regulation of membrane fusion.Glycoproteins gB and gH are required for syncytium formation but not for herpesvirus-induced nuclear envelope breakdown.Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdownPrimary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product.Pseudorabies virus glycoprotein K requires the UL20 gene product for processing.Pseudorabies virus glycoprotein M inhibits membrane fusion.Restoration of function of carboxy-terminally truncated pseudorabies virus glycoprotein B by point mutations in the ectodomain.The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virionsGlycoproteins required for entry are not necessary for egress of pseudorabies virus.Intracellular localization of the pseudorabies virus large tegument protein pUL36.Kaposi's sarcoma-associated herpesvirus gH/gL: glycoprotein export and interaction with cellular receptors.Relevance of the interaction between alphaherpesvirus UL3.5 and UL48 proteins for virion maturation and neuroinvasion.A pseudorabies virus recombinant simultaneously lacking the major tegument proteins encoded by the UL46, UL47, UL48, and UL49 genes is viable in cultured cells.Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein.Identification, subviral localization, and functional characterization of the pseudorabies virus UL17 protein.Pseudorabies virus UL3 gene codes for a nuclear protein which is dispensable for viral replication.The pseudorabies virus US3 protein is a component of primary and of mature virions.
P2860
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P2860
Glycoprotein gL-independent infectivity of pseudorabies virus is mediated by a gD-gH fusion protein
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Glycoprotein gL-independent in ...... ated by a gD-gH fusion protein
@en
Glycoprotein gL-independent in ...... ted by a gD-gH fusion protein.
@nl
type
label
Glycoprotein gL-independent in ...... ated by a gD-gH fusion protein
@en
Glycoprotein gL-independent in ...... ted by a gD-gH fusion protein.
@nl
prefLabel
Glycoprotein gL-independent in ...... ated by a gD-gH fusion protein
@en
Glycoprotein gL-independent in ...... ted by a gD-gH fusion protein.
@nl
P2860
P1433
P1476
Glycoprotein gL-independent in ...... ated by a gD-gH fusion protein
@en
P2093
T C Mettenleiter
P2860
P304
P407
P577
1999-04-01T00:00:00Z