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The IE180 protein of pseudorabies virus suppresses phosphorylation of translation initiation factor eIF2 alpha

(2012) JOURNAL OF VIROLOGY. 86(13). p.7235-7240
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Abstract
We have previously shown that the porcine alphaherpesvirus pseudorabies virus (PRY) efficiently interferes with phosphorylation of the eukaryotic translation initiation factor eIF2 alpha. Inhibition of phosphorylation of eIF2 alpha has been reported earlier for the closely related alphaherpesvirus herpes simplex virus 1 (HSV-1) through its ICP34.5 and US11 proteins. PRV, however, does not encode an ICP34.5 or US11 orthologue. Assays using cycloheximide, UV-inactivated PRY, or phosphonoacetic acid (PAA) showed that de novo expression of one or more (immediate) early viral protein(s) is required for interference with eIF2 alpha phosphorylation. In line with this, a time course assay showed that eIF2 alpha phosphorylation was abolished within 2 h after PRY inoculation. PRY encodes only one immediate-early protein, IE180, the orthologue of HSV-1 ICP4. As reported earlier, a combinational treatment of cells with cycloheximide and actinomycin D allowed expression of IE180 without detectable expression of the US3 early protein in PRV-infected cells. This led to a substantial reduction in eIF2 alpha phosphorylation levels, indicative for an involvement of IE180. In support of this, transfection of IE180 also potently reduced eIF2 alpha phosphorylation. IE180-mediated interference with eIF2 alpha phosphorylation was not cell type dependent, as it occurred both in rat neuronal 50B11 cells and in swine testicle cells. Inhibition of the cellular phosphatase PP1 impaired PRV-mediated interference with eIF2 alpha phosphorylation, indicating that PP1 is involved in this process. In conclusion, the immediate-early IE180 protein of PRY has the previously uncharacterized ability to suppress phosphorylation levels of the eukaryotic translation initiation factor eIF2 alpha.
Keywords
PROMOTER, EXPRESSION, INTERFERON, RNA, INHIBITION, TYPE-1, KINASE-R, INFECTED-CELLS, PHOSPHATASE 1, GAMMA(1)34.5 PROTEIN

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Citation

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MLA
Van Opdenbosch, Nina, Celine Van den Broeke, Nick De Regge, et al. “The IE180 Protein of Pseudorabies Virus Suppresses Phosphorylation of Translation Initiation Factor eIF2 Alpha.” JOURNAL OF VIROLOGY 86.13 (2012): 7235–7240. Print.
APA
Van Opdenbosch, N., Van den Broeke, C., De Regge, N., Tabarés, E., & Favoreel, H. (2012). The IE180 protein of pseudorabies virus suppresses phosphorylation of translation initiation factor eIF2 alpha. JOURNAL OF VIROLOGY, 86(13), 7235–7240.
Chicago author-date
Van Opdenbosch, Nina, Celine Van den Broeke, Nick De Regge, E Tabarés, and Herman Favoreel. 2012. “The IE180 Protein of Pseudorabies Virus Suppresses Phosphorylation of Translation Initiation Factor eIF2 Alpha.” Journal of Virology 86 (13): 7235–7240.
Chicago author-date (all authors)
Van Opdenbosch, Nina, Celine Van den Broeke, Nick De Regge, E Tabarés, and Herman Favoreel. 2012. “The IE180 Protein of Pseudorabies Virus Suppresses Phosphorylation of Translation Initiation Factor eIF2 Alpha.” Journal of Virology 86 (13): 7235–7240.
Vancouver
1.
Van Opdenbosch N, Van den Broeke C, De Regge N, Tabarés E, Favoreel H. The IE180 protein of pseudorabies virus suppresses phosphorylation of translation initiation factor eIF2 alpha. JOURNAL OF VIROLOGY. 2012;86(13):7235–40.
IEEE
[1]
N. Van Opdenbosch, C. Van den Broeke, N. De Regge, E. Tabarés, and H. Favoreel, “The IE180 protein of pseudorabies virus suppresses phosphorylation of translation initiation factor eIF2 alpha,” JOURNAL OF VIROLOGY, vol. 86, no. 13, pp. 7235–7240, 2012.
@article{2972503,
  abstract     = {We have previously shown that the porcine alphaherpesvirus pseudorabies virus (PRY) efficiently interferes with phosphorylation of the eukaryotic translation initiation factor eIF2 alpha. Inhibition of phosphorylation of eIF2 alpha has been reported earlier for the closely related alphaherpesvirus herpes simplex virus 1 (HSV-1) through its ICP34.5 and US11 proteins. PRV, however, does not encode an ICP34.5 or US11 orthologue. Assays using cycloheximide, UV-inactivated PRY, or phosphonoacetic acid (PAA) showed that de novo expression of one or more (immediate) early viral protein(s) is required for interference with eIF2 alpha phosphorylation. In line with this, a time course assay showed that eIF2 alpha phosphorylation was abolished within 2 h after PRY inoculation. PRY encodes only one immediate-early protein, IE180, the orthologue of HSV-1 ICP4. As reported earlier, a combinational treatment of cells with cycloheximide and actinomycin D allowed expression of IE180 without detectable expression of the US3 early protein in PRV-infected cells. This led to a substantial reduction in eIF2 alpha phosphorylation levels, indicative for an involvement of IE180. In support of this, transfection of IE180 also potently reduced eIF2 alpha phosphorylation. IE180-mediated interference with eIF2 alpha phosphorylation was not cell type dependent, as it occurred both in rat neuronal 50B11 cells and in swine testicle cells. Inhibition of the cellular phosphatase PP1 impaired PRV-mediated interference with eIF2 alpha phosphorylation, indicating that PP1 is involved in this process. In conclusion, the immediate-early IE180 protein of PRY has the previously uncharacterized ability to suppress phosphorylation levels of the eukaryotic translation initiation factor eIF2 alpha.},
  author       = {Van Opdenbosch, Nina and Van den Broeke, Celine and De Regge, Nick and Tabarés, E and Favoreel, Herman},
  issn         = {0022-538X},
  journal      = {JOURNAL OF VIROLOGY},
  keywords     = {PROMOTER,EXPRESSION,INTERFERON,RNA,INHIBITION,TYPE-1,KINASE-R,INFECTED-CELLS,PHOSPHATASE 1,GAMMA(1)34.5 PROTEIN},
  language     = {eng},
  number       = {13},
  pages        = {7235--7240},
  title        = {The IE180 protein of pseudorabies virus suppresses phosphorylation of translation initiation factor eIF2 alpha},
  url          = {http://dx.doi.org/10.1128/JVI.06929-11},
  volume       = {86},
  year         = {2012},
}

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