scholarly journals Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6

Aging ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 5751-5763
Author(s):  
Mingsheng Cai ◽  
Xiaowen Ou ◽  
Yiwen Li ◽  
Xingmei Zou ◽  
Zuo Xu ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Subcellular Localization ◽  
Nuclear Import ◽  
Herpes Simplex Virus 1 ◽  
Molecular Anatomy ◽  
Simplex Virus

Characterization of the nuclear import signal of herpes simplex virus 1 UL31

2016 ◽  
Vol 161 (9) ◽  
pp. 2379-2385 ◽  
Author(s):  
Mingsheng Cai ◽  
Daixiong Chen ◽  
Zhancheng Zeng ◽  
Hang Yang ◽  
Si Jiang ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Nuclear Import ◽  
Herpes Simplex Virus 1 ◽  
Simplex Virus

Characterization of the subcellular localization and nuclear import molecular mechanisms of herpes simplex virus 1 UL2

2017 ◽  
Vol 398 (4) ◽  
pp. 509-517 ◽  
Author(s):  
Mingsheng Cai ◽  
Zebin Huang ◽  
Zongmin Liao ◽  
Tao Chen ◽  
Ping Wang ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Subcellular Localization ◽  
Yellow Fluorescent Protein ◽  
Nuclear Accumulation ◽  
Live Cells ◽  
Cellular Transport ◽  
Herpes Simplex Virus 1 ◽  
Simplex Virus ◽  
Hsv 1

Abstract As a crucial protein, the herpes simplex virus 1 (HSV-1) UL2 protein has been shown to take part in various stages of viral infection, nonetheless, its exact subcellular localization and transport molecular determinants are not well known thus far. In the present study, by using live cells fluorescent microscopy assay, UL2 tagged with enhanced yellow fluorescent protein was transiently expressed in live cells and showed a completely nuclear accumulation without the presence of other HSV-1 proteins. Moreover, the nuclear transport of UL2 was characterized to be assisted by multiple transport pathways through Ran-, importin α1-, α5-, α7-, β1- and transportin-1 cellular transport receptors. Consequently, these results will improve understanding of UL2-mediated biological functions in HSV-1 infection cycles.

scholarly journals Herpes Simplex Virus 1 Protein Kinase Us3 and Major Tegument Protein UL47 Reciprocally Regulate Their Subcellular Localization in Infected Cells

2011 ◽  
Vol 85 (18) ◽  
pp. 9599-9613 ◽  
Author(s):  
A. Kato ◽  
Z. Liu ◽  
A. Minowa ◽  
T. Imai ◽  
M. Tanaka ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Protein Kinase ◽  
Subcellular Localization ◽  
Tegument Protein ◽  
Herpes Simplex Virus 1 ◽  
Infected Cells ◽  
Simplex Virus

scholarly journals Identification of Two Nuclear Import Signals in the α-Gene Product ICP22 of Herpes Simplex Virus 1

Virology ◽  
2002 ◽  
Vol 295 (2) ◽  
pp. 360-370 ◽  
Author(s):  
Gerhard Stelz ◽  
Elke Rücker ◽  
Olaf Rosorius ◽  
Gerold Meyer ◽  
Roland H. Stauber ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Gene Product ◽  
Nuclear Import ◽  
Herpes Simplex Virus 1 ◽  
Simplex Virus

Assembly of VP26 in herpes simplex virus-1 capsid implicated by 3-D structure of recombinant capsid

1995 ◽  
Vol 53 ◽  
pp. 840-841
Author(s):  
Z. Hong Zhou ◽  
Jing He ◽  
Joanita Jakana ◽  
J. D. Tatman ◽  
Frazer J. Rixon ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
3D Structure ◽  
Structure Study ◽  
Herpes Simplex Virus 1 ◽  
Shell Proteins ◽  
Life Threatening ◽  
Infected Cells ◽  
Simplex Virus ◽  
Hsv 1

Herpes simplex virus-1 (HSV-1) is a ubiquitous virus which is implicated in diseases ranging from self-curing cold sores to life-threatening infections. The 2500 Å diameter herpes virion is composed of a glycoprotein spike containing, lipid envelope, enclosing a protein layer (the tegument) in which is embedded the capsid (which contains the dsDNA genome). The B-, and A- and C-capsids, representing different morphogenetic stages in HSV-1 infected cells, are composed of 7, and 5 structural proteins respectively. The three capsid types are organized in similar T=16 icosahedral shells with 12 pentons, 150 hexons, and 320 connecting triplexes. Our previous 3D structure study at 26 Å revealed domain features of all these structural components and suggested probable locations for the outer shell proteins, VP5, VP26, VP19c and VP23. VP5 makes up most of both pentons and hexons. VP26 appeared to bind to the VP5 subunit in hexon but not to that in penton.

Ultraviolet Light Induces Reactivation in a Murine Model of Cutaneous Herpes Simplex Virus-1 Infection¶

2001 ◽  
Vol 74 (1) ◽  
pp. 108 ◽  
Author(s):  
Diane E. Goade ◽  
Robert A. Nofchissey ◽  
Donna F. Kusewitt ◽  
Brian Hjelle ◽  
John Kreisel ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ultraviolet Light ◽  
Murine Model ◽  
Herpes Simplex Virus 1 ◽  
Simplex Virus
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