Isolation of high-molecular-weight infectious DNA from type 1 herpes simplex virus

1977 ◽  
Vol 83 (1) ◽  
pp. 28-31
Author(s):  
F. P. Filatov ◽  
A. A. Manykin ◽  
L. A. Monastyreva
Keyword(s):  
Molecular Weight ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
High Molecular Weight ◽  
Simplex Virus

scholarly journals AlaArg Motif in the Carboxyl Terminus of the γ134.5 Protein of Herpes Simplex Virus Type 1 Is Required for the Formation of a High-Molecular-Weight Complex That Dephosphorylates eIF-2α

2001 ◽  
Vol 75 (8) ◽  
pp. 3666-3674 ◽  
Author(s):  
Guofeng Cheng ◽  
Martin Gross ◽  
Marie-Elena Brett ◽  
Bin He
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
High Molecular Weight ◽  
Translation Initiation Factor ◽  
Carboxyl Terminus ◽  
High Molecular Weight Complex ◽  
Simplex Virus

ABSTRACT The γ134.5 protein of herpes simplex virus (HSV) type 1 functions to prevent the shutoff of protein synthesis mediated by the double-stranded-RNA-dependent protein kinase PKR. This is because γ134.5 associates with protein phosphatase 1 (PP1) through its carboxyl terminus, forming a high-molecular-weight complex that dephosphorylates the α subunit of translation initiation factor eIF-2 (eIF-2α). Here we show that Val193Glu and Phe195Leu substitutions in the PP1 signature motif of the γ134.5 protein abolished its ability to redirect PP1 to dephosphorylate eIF-2α and replication of mutant viruses was severely impaired. The γ134.5 protein, when expressed in Sf9 cells using a recombinant baculovirus, was capable of directing specific eIF-2α dephosphorylation. Deletions of amino acids 258 to 263 had no effect on activity of γ134.5. However, deletions of amino acids 238 to 258 abolished eIF-2α phosphatase activity but not PP1 binding activity. Interestingly, deletions in the AlaArg motif of the carboxyl terminus disrupted the high-molecular-weight complex that is required for dephosphorylation of eIF-2α. These results demonstrate that γ134.5 is functionally active in the absence of any other HSV proteins. In addition to a PP1 binding domain, the carboxyl terminus of γ134.5 contains an effector domain that is required to form a functional complex.

Low-molecular weight mannogalactofucans prevent herpes simplex virus type 1 infection via activation of Toll-like receptor 2

2017 ◽  
Vol 103 ◽  
pp. 286-293 ◽  
Author(s):  
Woo Jung Kim ◽  
Ji Won Choi ◽  
Won Jong Jang ◽  
Young-Sun Kang ◽  
Chang Won Lee ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Low Molecular Weight ◽  
Toll Like Receptor ◽  
Toll Like Receptor 2 ◽  
Simplex Virus

Role of herpes simplex virus type 1 (HSV-1) in the pathogenesis of peptic ulcer disease

2001 ◽  
Vol 120 (5) ◽  
pp. A136-A137
Author(s):  
K TSAMAKIDES ◽  
E PANOTOPOULOU ◽  
D DIMITROULOPOULOS ◽  
M CHRISTOPOULO ◽  
D XINOPOULOS ◽  
...  
Keyword(s):  
Peptic Ulcer ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Peptic Ulcer Disease ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Ulcer Disease ◽  
Simplex Virus
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