Journal of Virology
Geisel School of Medicine
Cells use the interferon-induced, double-stranded-RNA-dependent protein kinase PKR as a defense against virus infections. Upon activation, PKR phosphorylates and thereby inactivates the protein synthesis initiation factor eIF-2, resulting in the cessation of protein synthesis. Viruses have evolved various strategies to counteract this cellular defense. In this paper, we show that simian virus 40 (SV40) large-T antigen can antagonize the translational inhibitory effect resulting from the activation of PKR in virus-infected cells. Unlike the situation with other virus-host cell interactions, SV40 large-T antigen does not block the activation of PKR, suggesting that SV40 counteracts the cellular antiviral response mediated by PKR at a step downstream of PKR activation. Mutational analysis of large-T antigen indicates that a domain located between amino acids 400 and 600 of large-T antigen is responsible for this function. These results define a novel translational regulatory function for the SV40 large-T antigen.
Rajan P, Swaminathan S, Zhu J, et al. A novel translational regulation function for the simian virus 40 large-T antigen gene. J Virol. 1995;69(2):785-795. doi:10.1128/JVI.69.2.785-795.1995
Dartmouth Digital Commons Citation
Rajan, Prithi; Swaminathan, Sathyamagalam; Zhu, Jiyue; and Cole, Charles N., "A Novel Translational Regulation Function for the Simian Virus 40 Large-T Antigen Gene." (1995). Dartmouth Scholarship. 1135.