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J. Virol., Feb 1995, 785-795, Vol 69, No. 2
Copyright © 1995, American Society for Microbiology

A novel translational regulation function for the simian virus 40 large- T antigen gene

P Rajan, S Swaminathan, J Zhu, CN Cole, G Barber, MJ Tevethia and B Thimmapaya
Robert H. Lurie Cancer Center, Northwestern University Medical School, Chicago, Illinois 60611.

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.

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