Herpes simplex virus tegument protein VP22 contains an internal VP16 interaction domain and a C-terminal domain that are both required for VP22 assembly into the virus particle.
about
Direct and specific binding of the UL16 tegument protein of herpes simplex virus to the cytoplasmic tail of glycoprotein E.Herpes simplex virus 1 VP22 regulates translocation of multiple viral and cellular proteins and promotes neurovirulence.Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase.VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamiliesVirion 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.The amino terminus of the herpes simplex virus 1 protein Vhs mediates membrane association and tegument incorporation.ORF11 protein interacts with the ORF9 essential tegument protein in varicella-zoster virus infectionThe herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner.RNA binding by the herpes simplex virus type 1 nucleocytoplasmic shuttling protein UL47 is mediated by an N-terminal arginine-rich domain that also functions as its nuclear localization signal.The varicella-zoster virus (VZV) ORF9 protein interacts with the IE62 major VZV transactivator.Recruitment of herpes simplex virus type 1 immediate-early protein ICP0 to the virus particle.A network of protein interactions around the herpes simplex virus tegument protein VP22.Virion incorporation of the herpes simplex virus type 1 tegument protein VP22 occurs via glycoprotein E-specific recruitment to the late secretory pathway.A conserved carboxy-terminal domain in the major tegument structural protein VP22 facilitates virion packaging of a chimeric protein during productive herpes simplex virus 1 infection.Functional homologies between avian and human alphaherpesvirus VP22 proteins in cell-to-cell spreading as revealed by a new cis-complementation assay.Multiple post-transcriptional strategies to regulate the herpes simplex virus type 1 vhs endoribonuclease
P2860
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P2860
Herpes simplex virus tegument protein VP22 contains an internal VP16 interaction domain and a C-terminal domain that are both required for VP22 assembly into the virus particle.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Herpes simplex virus tegument ...... embly into the virus particle.
@en
type
label
Herpes simplex virus tegument ...... embly into the virus particle.
@en
prefLabel
Herpes simplex virus tegument ...... embly into the virus particle.
@en
P2093
P2860
P1433
P1476
Herpes simplex virus tegument ...... embly into the virus particle.
@en
P2093
Emmanuelle Bernard
Gillian Elliott
Rachelle Cook
Wali Hafezi
P2860
P304
13082-13093
P356
10.1128/JVI.79.20.13082-13093.2005
P407
P577
2005-10-01T00:00:00Z