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Abstract
BackgroundDevelopment of compensatory mutations within the HIV p7/p1 and p1/p6 protease cleavage site region has been observed in HIV-infected patients treated with protease inhibitors. Mechanisms of fitness compensation may occur in HCV populations upon treatment of HCV protease inhibitors as well.FindingsIn this study, we investigated whether substitutions in protease cleavage site regions of HCV occur in response to a treatment regimen containing the NS3/4A protease inhibitor telaprevir (TVR). Evaluation of viral populations from 569 patients prior to treatment showed that the four NS3/4A cleavage sites were well conserved. Few changes in the cleavage site regions were observed in the 159 patients who failed TVR combination treatment, and no residues displayed evidence of directional selection after the acquisition of TVR-resistance.ConclusionsCleavage site mutations did not occur after treatment with the HCV protease inhibitor telaprevir.
Highlights
Development of compensatory mutations within the Human immunodeficiency virus (HIV) p7/p1 and p1/p6 protease cleavage site region has been observed in HIV-infected patients treated with protease inhibitors
Cleavage site mutations did not occur after treatment with the Hepatitis C virus (HCV) protease inhibitor telaprevir
During HIV Protease inhibitors (PI) treatment, in addition to the primary resistant variants observed in the catalytic site of the protease, variants have been observed within the protease substrates of p7/p1 and p1/p6 of the Gag-Pol polyprotein
Summary
Development of compensatory mutations within the HIV p7/p1 and p1/p6 protease cleavage site region has been observed in HIV-infected patients treated with protease inhibitors. Phase 3 clinical studies investigating TVR combination treatment demonstrated significant improvement of sustained viral response (SVR) rates compared to peginterferon alfa-2a and ribavirin alone (PR) in HCV genotype 1 infected patients [5,6]. We sought to determine if cleavage site mutations occur, either in the presence or absence of catalytic site mutations in the HCV NS3/4A protease, to improve the processing capacity of the protease as observed during HIV infection treatment.
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