Template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase.

ABSTRACT: During reverse transcription of the HIV-1 genome, two strand-transfer events occur. Both events rely on the RNase H cleavage activity of reverse transcriptases (RTs) and template homology. Using a panel of mutants of HIV-1_BH10 (group M/subtype B) and HIV-1_ESP49 (group O) RTs and in vitro assays, we demonstrate that there is a strong correlation between RT minus-strand transfer efficiency and template-primer binding affinity. The highest strand transfer efficiencies were obtained with HIV-1_ESP49 RT mutants containing the substitutions K358R/A359G/S360A, alone or in combination with V148I or T355A/Q357M. These HIV-1_ESP49 RT mutants had been previously engineered to increase their DNA polymerase activity at high temperatures. Now, we found th

SUBMITTER: Luczkowiak J 

PROVIDER: S-EPMC6120193 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature