Protein kinase R (PKR) plays a pro-viral role in porcine reproductive and respiratory syndrome virus (PRRSV) replication by modulating viral gene transcription

Protein kinase R (PKR) plays a pro-viral role in porcine reproductive and respiratory syndrome... Protein kinase R (PKR) is involved in apoptotic cell death and antiviral activities in response to many virus infections. To reveal the role of PKR in the replication of porcine reproductive and respiratory syndrome virus (PRRSV), we first examined the kinetics of PKR phosphorylation during PRRSV infection. The results showed that PRRSV transiently activates PKR at 12 and 24 h postinfection. Surprisingly, eIF-2α, the well-known downstream target of PKR, was significantly phosphorylated compared to mock-infected cells only at 48 and 72 h postinfection. Reduced viral gene transcription, viral protein synthesis, and virus titer were detected in cells transfected with PKR silencing RNA prior to PRRSV infection compared to control silencing RNA transfected cells, indicating a role of PKR in facilitating virus replication. Overall, our data suggest that PKR is not a major contributor to the phosphorylation of eIF-2α during PRRSV infection, but it plays a pro-viral role in PRRSV replication by modulating primarily viral gene transcription. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Protein kinase R (PKR) plays a pro-viral role in porcine reproductive and respiratory syndrome virus (PRRSV) replication by modulating viral gene transcription

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Publisher
Springer Vienna
Copyright
Copyright © 2016 by Springer-Verlag Wien
Subject
Biomedicine; Virology; Medical Microbiology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-015-2671-0
Publisher site
See Article on Publisher Site

Abstract

Protein kinase R (PKR) is involved in apoptotic cell death and antiviral activities in response to many virus infections. To reveal the role of PKR in the replication of porcine reproductive and respiratory syndrome virus (PRRSV), we first examined the kinetics of PKR phosphorylation during PRRSV infection. The results showed that PRRSV transiently activates PKR at 12 and 24 h postinfection. Surprisingly, eIF-2α, the well-known downstream target of PKR, was significantly phosphorylated compared to mock-infected cells only at 48 and 72 h postinfection. Reduced viral gene transcription, viral protein synthesis, and virus titer were detected in cells transfected with PKR silencing RNA prior to PRRSV infection compared to control silencing RNA transfected cells, indicating a role of PKR in facilitating virus replication. Overall, our data suggest that PKR is not a major contributor to the phosphorylation of eIF-2α during PRRSV infection, but it plays a pro-viral role in PRRSV replication by modulating primarily viral gene transcription.

Journal

Archives of VirologySpringer Journals

Published: Feb 1, 2016

References

  • HIV-I TAT inhibits PKR activity by both RNA-dependent and RNA-independent mechanisms
    Cai, R; Carpick, B; Chun, RF; Jeang, KT; Williams, BR
  • Regulation of stress granules and P-bodies during RNA virus infection
    Lloyd, RE
  • Inhibition of porcine reproductive and respiratory syndrome virus by interferon-gamma and recovery of virus replication with 2-aminopurine
    Rowland, RR; Robinson, B; Stefanick, J; Kim, TS; Guanghua, L; Lawson, SR; Benfield, DA
  • Porcine reproductive and respiratory syndrome virus productively infects monocyte-derived dendritic cells and compromises their antigen-presenting ability
    Wang, X; Eaton, M; Mayer, M; Li, H; He, D; Nelson, E; Christopher-Hennings, J
  • Role of phosphatidylinositol 3-kinase (PI3K) and Akt1 kinase in porcine reproductive and respiratory syndrome virus (PRRSV) replication
    Wang, X; Zhang, H; Abel, AM; Young, AJ; Xie, L; Xie, Z
  • Porcine reproductive and respiratory syndrome virus activates the transcription of interferon alpha/beta (IFN-alpha/beta) in monocyte-derived dendritic cells (Mo-DC)
    Zhang, H; Guo, X; Nelson, E; Christopher-Hennings, J; Wang, X

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