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Virologie

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HIV-1 gag cleavage sites and resistance to protease inhibitors Volume 14, issue 2, mars-avril 2010

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Authors
Hôpital Bichat-Claude-Bernard, Université Paris-Diderot-Paris-VII, Laboratoire de virologie, EA 4409, 46, rue Henri-Huchard, 75018 Paris, France

The role of the human immunodeficiency virus type 1 protease is to cleave gag and Gag-pol polyproteinic precursors at specific sites called cleavage sites to liberate the structural proteins (p7, p17 and p24) and enzymes (protease, reverse transcriptase and integrase) of the virus. Ribosomal –1 frameshifting mediated by a downstream signal is required for translating the messenger RNA in these precursors. At time of virological failure, mutations associated with resistance to PI in protease gene are selected. These substitutions are responsible for a decrease in viral replicative capacity. Mutations at gag cleavage sites can be selected in virus from patients failing PI containing regimen. Studies have shown that presence of gag cleavage sites substitutions in the absence of mutations in the protease gene might be associated with virological failure.