Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
about
Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Macrophages and cytokines in the early defence against herpes simplex virusUs9-Independent Axonal Sorting and Transport of the Pseudorabies Virus Glycoprotein gM.Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro.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.Identification and characterization of the pseudorabies virus tegument proteins UL46 and UL47: role for UL47 in virion morphogenesis in the cytoplasm.Epstein-Barr virus that lacks glycoprotein gN is impaired in assembly and infectionPseudorabies virus UL37 gene product is involved in secondary envelopment.Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions.Pseudorabies virus pUL46 induces activation of ERK1/2 and regulates herpesvirus-induced nuclear envelope breakdown.The UL7 gene of pseudorabies virus encodes a nonessential structural protein which is involved in virion formation and egress.Directed egress of animal viruses promotes cell-to-cell spreadA subpopulation of tegument protein vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells.Herpesvirus assembly and egressVaricella-zoster virus open reading frame 10 is a virulence determinant in skin cells but not in T cells in vivoHuman cytomegalovirus UL97 kinase and nonkinase functions mediate viral cytoplasmic secondary envelopment.Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49.Growth, physicochemical properties, and morphogenesis of Chinese wild-type PRV Fa and its gene-deleted mutant strain PRV SA215.Herpes simplex virus glycoproteins gB and gD function in a redundant fashion to promote secondary envelopmentProteomic characterization of pseudorabies virus extracellular virionsEssential functions of the unique N-terminal region of the varicella-zoster virus glycoprotein E ectodomain in viral replication and in the pathogenesis of skin infectionHerpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm.Interaction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gDVirion incorporation of the herpes simplex virus type 1 tegument protein VP22 is facilitated by trans-Golgi network localization and is independent of interaction with glycoprotein E.Varicella-zoster virus glycoprotein M homolog is glycosylated, is expressed on the viral envelope, and functions in virus cell-to-cell spreadEpstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.Deletion of the first cysteine-rich region of the varicella-zoster virus glycoprotein E ectodomain abolishes the gE and gI interaction and differentially affects cell-cell spread and viral entry.Rise and survival of bovine herpesvirus 1 recombinants after primary infection and reactivation from latencyGlycoproteins gE and gI are required for efficient KIF1A-dependent anterograde axonal transport of alphaherpesvirus particles in neurons.EBV BMRF-2 facilitates cell-to-cell spread of virus within polarized oral epithelial cells.Nuclear Exodus: Herpesviruses Lead the Way.EBV-positive human sera contain antibodies against the EBV BMRF-2 protein.Herpes simplex virus type 1 glycoprotein K and the UL20 protein are interdependent for intracellular trafficking and trans-Golgi network localizationHerpesviruses remodel host membranes for virus egress.Glycoproteins gB and gH are required for syncytium formation but not for herpesvirus-induced nuclear envelope breakdown.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.Assembly and organization of glycoproteins B, C, D, and H in herpes simplex virus type 1 particles lacking individual glycoproteins: No evidence for the formation of a complex of these molecules.Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread.
P2860
Q24531303-7E83033A-6F3A-484B-B51E-3528D3A13F01Q24815062-2A5D072B-35D5-45C1-B5E6-4C3DADE27877Q27321519-B699D186-A9E6-48C2-BCFA-4FE42457EC34Q30477354-54B2B112-DFA5-47C7-AFE7-65CF384100C2Q31032273-9FD73DA7-2B4C-4469-826F-EE5FE7A4C1A6Q32181899-2B4D5C5A-D896-42F2-930C-824774C34A8EQ33826978-ADA99542-FEE4-4F84-AED7-FAEBD1A71093Q33844984-4C08E488-1E32-4144-AFD0-4830767E7C7CQ33855020-7F2FD4DF-ABD6-42EE-867E-87ECFAB72C66Q33887668-6B121D10-861A-4187-80F7-9B82BF5C0381Q33930460-7A28CCF9-C60F-487E-B67C-C62EF8585F4BQ34327423-0B846288-DC86-405B-A920-2E3E95E32DF2Q34468903-7646B976-5AAA-4596-B777-ECDA83B269CBQ34499618-14B451C1-5078-4506-83A7-079093578717Q34545651-3BAAF899-A07D-4D88-97F3-2793C7E7974CQ34742654-32E52E62-0AFC-44AB-BF9F-B02FF6F8D1ACQ35000306-E738C17B-784A-4645-9A5A-B4C685BFAAE1Q35061500-9B3D4021-91CF-4DEC-BB53-CBA122312990Q35076641-75FA931B-1C78-4197-8BF3-9B61D567A104Q35077562-70101EA5-D837-4BAC-BFA5-4FA040D2974AQ35101360-DAD4D723-997B-4A28-8971-00F58BFE317FQ35155202-7FFFAFEA-2CC6-4889-9C09-4233EEB4265BQ35192694-3D749EF8-49B7-4F4A-8B38-49E421648EB2Q35634281-2FBCB0F7-2022-4DB5-99D8-6A8AA99B2C16Q36304865-BF54059D-2F78-4117-8CCD-016C034A4E99Q36424473-B2E7B587-8B01-48F6-AC91-9E09A24B7FBFQ36600329-E2704ECB-8BB9-4FAC-82DC-326407E91DCFQ37033241-2B69CCA6-A26C-4BAF-AA0F-FC9AE50A5478Q37060076-FA5E9B52-CEB7-4BA9-8DAF-54E7CEA7BC1FQ37123566-92D040E2-8D65-43E0-9AF2-879943B23621Q37303761-263971ED-F918-4D3F-BB3C-B0901F82F1B9Q37341587-200A7C11-5EDE-45E6-A507-6C7AB33CA83DQ37408295-22813A9C-1F44-45FC-9265-5EB316E1918DQ37596504-F9BD440C-9C2C-45BC-97CD-DD4C888721B6Q37865385-83E8F768-EEE0-4940-966C-038F53EC8992Q39130840-F89E1801-5852-4915-A817-553AFBFC67C4Q39366626-67A20BC3-B9AA-4B57-9739-A540696D9E83Q39539545-3F6B98C1-6B0B-4C1A-91F9-5328FCC195C8Q39601462-7124FE16-4493-4D56-8463-35F533D01DC7Q39601524-50B5CF6C-6E33-4AC6-B1F2-550CB9640861
P2860
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@ast
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@en
type
label
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@ast
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@en
prefLabel
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@ast
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@en
P2093
P2860
P1433
P1476
Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation.
@en
P2093
L W Enquist
R Tirabassi
T C Mettenleiter
P2860
P304
P356
10.1128/JVI.74.9.4004-4016.2000
P577
2000-05-01T00:00:00Z