scholarly journals Tsg101 Interacts with Herpes Simplex Virus 1 VP1/2 and Is a Substrate of VP1/2 Ubiquitin-Specific Protease Domain Activity

2012 ◽  
Vol 87 (1) ◽  
pp. 692-696 ◽  
Author(s):  
M. Caduco ◽  
A. Comin ◽  
M. Toffoletto ◽  
D. Munegato ◽  
E. Sartori ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Protease Domain ◽  
Herpes Simplex Virus 1 ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Simplex Virus

scholarly journals Tsg101 Interacts with Herpes Simplex Virus 1 VP1/2 and Is a Substrate of VP1/2 Ubiquitin-Specific Protease Domain Activity

2013 ◽  
Vol 87 (11) ◽  
pp. 6537-6537
Author(s):  
M. Caduco ◽  
A. Comin ◽  
M. Toffoletto ◽  
D. Munegato ◽  
E. Sartori ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Protease Domain ◽  
Herpes Simplex Virus 1 ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Simplex Virus

scholarly journals Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1

2015 ◽  
Vol 290 (38) ◽  
pp. 22907-22918 ◽  
Author(s):  
Alexandra K. Pozhidaeva ◽  
Kareem N. Mohni ◽  
Sirano Dhe-Paganon ◽  
Cheryl H. Arrowsmith ◽  
Sandra K. Weller ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Herpes Simplex Virus 1 ◽  
Early Protein ◽  
Human Ubiquitin ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Protein Icp0 ◽  
Simplex Virus

scholarly journals Ubiquitin-specific protease 9X in host cells interacts with herpes simplex virus 1 ICP0

2016 ◽  
Vol 78 (3) ◽  
pp. 405-410 ◽  
Author(s):  
Yuka SATO ◽  
Akihisa KATO ◽  
Jun ARII ◽  
Naoto KOYANAGI ◽  
Hiroko KOZUKA-HATA ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Host Cells ◽  
Herpes Simplex Virus 1 ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Simplex Virus

scholarly journals The Ability of Herpes Simplex Virus Type 1 Immediate-Early Protein Vmw110 To Bind to a Ubiquitin-Specific Protease Contributes to Its Roles in the Activation of Gene Expression and Stimulation of Virus Replication

1999 ◽  
Vol 73 (1) ◽  
pp. 417-426 ◽  
Author(s):  
Roger D. Everett ◽  
Michayla Meredith ◽  
Anne Orr
Keyword(s):  
Gene Expression ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Herpes Simplex Virus Type ◽  
Transfected Cells ◽  
Early Protein ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Simplex Virus

ABSTRACT Herpes simplex virus type 1 immediate-early protein Vmw110 stimulates the onset of virus infection and is required for efficient reactivation from latency. In transfection assays, Vmw110 is a potent activator of gene expression, but its mode of action has yet to be determined. Previous work has shown that Vmw110 localizes to specific intranuclear structures known as ND10, PML bodies, or PODs and causes the disruption of these domains. The ability of Vmw110 to disrupt ND10 correlates with its biological activities in infected and transfected cells. It has also been found that Vmw110 binds strongly and specifically to a ubiquitin-specific protease known as HAUSP, itself a component of a subset of ND10. In this study we have investigated the role of HAUSP in Vmw110 activity; single amino acid residues of Vmw110 required for the interaction were identified, and the effects of mutation of these residues in infected and transfected cells were then assayed. The results indicate that the ability to bind to HAUSP contributes to the functional activities of Vmw110.

scholarly journals Reciprocal Activities between Herpes Simplex Virus Type 1 Regulatory Protein ICP0, a Ubiquitin E3 Ligase, and Ubiquitin-Specific Protease USP7

2005 ◽  
Vol 79 (19) ◽  
pp. 12342-12354 ◽  
Author(s):  
Chris Boutell ◽  
Mary Canning ◽  
Anne Orr ◽  
Roger D. Everett
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Regulatory Protein ◽  
Ring Finger ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Protein Icp0 ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 stimulates lytic infection and the reactivation of quiescent viral genomes. These roles of ICP0 require its RING finger E3 ubiquitin ligase domain, which induces the degradation of several cellular proteins, including components of promyelocytic leukemia nuclear bodies and centromeres. ICP0 also interacts very strongly with the cellular ubiquitin-specific protease USP7 (also known as HAUSP). We have shown previously that ICP0 induces its own ubiquitination and degradation in a RING finger-dependent manner, and that its interaction with USP7 regulates this process. In the course of these studies we found and report here that ICP0 also targets USP7 for ubiquitination and proteasome-dependent degradation. The reciprocal activities of the two proteins reveal an intriguing situation that poses the question of the balance of the two processes during productive HSV-1 infection. Based on a thorough analysis of the properties of an HSV-1 mutant virus that expresses forms of ICP0 that are unable to bind to USP7, we conclude that USP7-mediated stabilization of ICP0 is dominant over ICP0-induced degradation of USP7 during productive HSV-1 infection. We propose that the biological significance of the ICP0-USP7 interaction may be most pronounced in natural infection situations, in which limited amounts of ICP0 are expressed.

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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