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Published April 1, 1989 | Published
Journal Article Open

Human immunodeficiency virus tat-activated expression of poliovirus protein 2A inhibits mRNA translation

Abstract

To study the effect of poliovirus protein 2A on cellular RNA translation, the tat control system of human immunodeficiency virus (HIV) was used. Protein 2A was expressed from a plasmid construct (pHIV/2A) incorporating the HIV long terminal repeat. Protein synthesis was measured by using chloramphenicol acetyltransferase as a reporter gene driven by the Rous sarcoma virus long terminal repeat. When HIV/2A was contransfected with the reporter, addition of a tat-producing plasmid caused at least a 50-fold drop in chloramphenicol acetyltransferase synthesis. A HeLa cell line carrying HIV/2A was established. In it, tat expression caused more than a 10-fold drop in chloramphenicol acetyltransferase synthesis from the reporter plasmid. Furthermore, 2A induction by tat caused cleavage of the cellular translation factor P220, a part of eukaryotic translation initiation factor 4F. Thus protein 2A can, by itself, carry out the inhibition of cellular protein synthesis characteristic of a poliovirus infection. Also, the HIV tat activation provides a very effective method to control gene expression in mammalian cells.

Additional Information

© 1989 by the National Academy of Sciences. Contributed by David Baltimore, December 19, 1988. We thank Jing-po Li, Didier Trono, and Raul Andino for suggestions, Nahum Sonenberg for the anti-P220 serum, and Sunyoung Kim for the HIV/CAT plasmid. This work was supported by grants from the National Institute of Allergy and Infectious Diseases and the National Institute of General Medical Sciences. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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August 22, 2023
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