IMR Press / FBL / Volume 14 / Issue 7 / DOI: 10.2741/3408

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Role of RNA structure and protein factors in the control of HIV-1 splicing
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1 MAEM, UMR 7567 CNRS-UHP, Nancy Universite, Faculte des sciences et techniques, BP239, Vandoeuvre Les Nancy CEDEX, France
2 IGBMC, Department of Functional Genomics, Illkirch, F-67400, France
3 INSERM, U596, Illkirch, F-67400, France
4 CNRS, UMR7104, Illkirch, F-67400, France
5 Universite Louis Pasteur, Strasbourg, F-67000, France
Academic Editor:Zhi-Ming Zheng
Front. Biosci. (Landmark Ed) 2009, 14(7), 2714–2729;
Published: 1 January 2009
(This article belongs to the Special Issue Protein-RNA interactions in viral RNA processing)

Alternative splicing plays a key role in the production of numerous proteins by complex lentiviruses such as HIV-1. The study of HIV-1 RNA splicing has provided useful information not only about the physiology of the virus, but also about the general mechanisms that regulate mammalian pre-mRNA alternative splicing. Like all retroviruses, a fraction of HIV-1 transcripts remains intact to serve as genomic RNA and to code for Gag and Gag-Pol protein precursors. In addition, splicing is important for controlling the production of some viral proteins, which could otherwise have a negative effect on the infected cell. Here, we summarize how the utilization of HIV-1 splicing sites is limited by the binding of nuclear factors to cis-acting silencer elements, taking into account the role of RNA secondary structure in these mechanisms. We also describe how the poorly efficient HIV-1 acceptor sites are nevertheless activated by serine/arginine-rich proteins. Finally, we discuss how nuclear factors that interact with both the transcription and splicing machineries also participate in the control of HIV-1 RNA splicing.

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