The UL13 virion protein of herpes simplex virus type 1 is phosphorylated by a novel virus-induced protein kinase

ABSTRACT The herpes simplex virus type 1 γ134.5 gene product precludes the host-mediated protein shutoff response induced by activated protein kinase R (PKR). Earlier studies demonstrated that recombinant viruses lacking the γ134.5 gene (Δγ134.5) developed secondary mutations that allowed earlier US11 expression and enabled continued protein synthesis. Further, in vitro studies demonstrated that a recombinant expressed US11 protein binds PKR, blocks the phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF-2α) by activated PKR, and, if provided prior to PKR activation, precluded PKR autophosphorylation. The present study furthers the hypothesis that early US11 production precludes PKR-mediated host protein shutoff by demonstrating that (i) US11 and PKR interact in the context of viral infection, (ii) this interaction is RNA dependent and requires a 30-amino-acid domain (amino acids 91 to 121) in the carboxyl domain of the US11 protein, (iii) the proteins biochemically colocalize in the S100 ribosomal fraction, and (iv) there is a PKR substrate domain immediately adjacent to the binding domain. The results suggest that the US11 interaction with PKR at the ribosome is RNA dependent and that the US11 protein contains a substrate domain with homology to eIF-2α in close proximity to an essential binding domain.

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Molecular mechanism by which Us3 protein kinase regulates the pathogenicity of herpes simplex virus type-1

Uirusu ◽

10.2222/jsv.66.83 ◽

2016 ◽

Vol 66 (1) ◽

pp. 83-90 ◽

Cited By ~ 1

Author(s):

Akihisa KATO

Keyword(s):

Herpes Simplex Virus ◽

Herpes Simplex ◽

Protein Kinase ◽

Molecular Mechanism ◽

Virus Type ◽

Herpes Simplex Virus Type ◽

Simplex Virus

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Gene UL11 of Herpes Simplex Virus Type 1 Encodes a Virion Protein which Is Myristylated

Journal of General Virology ◽

10.1099/0022-1317-70-12-3147 ◽

1989 ◽

Vol 70 (12) ◽

pp. 3147-3157 ◽

Cited By ~ 47

Author(s):

C. A. MacLean ◽

B. Clark ◽

D. J. McGeoch

Keyword(s):

Herpes Simplex Virus ◽

Herpes Simplex ◽

Virus Type ◽

Herpes Simplex Virus Type ◽

Virion Protein ◽

Simplex Virus

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The Herpes Simplex Virus Type 1 DNA Packaging Protein UL17 Is a Virion Protein That Is Present in Both the Capsid and the Tegument Compartments

Journal of Virology ◽

10.1128/jvi.79.1.150-158.2005 ◽

2005 ◽

Vol 79 (1) ◽

pp. 150-158 ◽

Cited By ~ 47

Author(s):

Johanna K. Thurlow ◽

Frazer J. Rixon ◽

Mary Murphy ◽

Paul Targett-Adams ◽

Michelle Hughes ◽

...

Keyword(s):

Herpes Simplex Virus ◽

Herpes Simplex ◽

Virus Particle ◽

Virus Type ◽

Herpes Simplex Virus Type ◽

Virion Protein ◽

Mature Virus Particle ◽

Simplex Virus ◽

A Minor

ABSTRACT The UL17 protein of herpes simplex virus type 1 is essential for packaging the viral genome into the procapsid, a spherical assembly intermediate, and is present in the mature virus particle. We have examined the distribution of UL17 in various assembly products and virions to determine which component of the virus particle UL17 is associated with and at what stage in capsid assembly UL17 is required. UL17 was present in the procapsid, in the DNA-containing angularized C capsid, and in two other angularized capsid forms, A and B, that lack DNA and are thought to be dead-end products. The results suggest that UL17 is a minor capsid protein which is incorporated into the procapsid during assembly of the particle. UL17 was also found in virions and in noninfectious structures known as light (L) particles, which possess a tegument and envelope but lack a capsid. The level of UL17 in these particles was much greater than the amount that could be attributed to capsid contamination of the purified L-particle preparation, suggesting that UL17 is also a tegument protein. The finding that virions contain approximately twofold more UL17 than do C capsids provided further support for the idea that UL17 is present in two different structural components within the mature virion. The UL25 packaging protein, which is also present in virions, was not found in significant amounts in L particles, indicating that it is associated only with the capsid. UL6, the third virion-associated packaging protein, was present in slightly increased levels in L particles.

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