Analysis of mutations at positions 115 and 116 in the dNTP binding site of HIV-1 reverse transcriptase

AUTOR(ES)

Boyer, Paul L.

FONTE

The National Academy of Sciences

RESUMO

We have examined amino acid substitutions at residues 115 and 116 in the reverse transcriptase (RT) of HIV-1. A number of properties were examined, including polymerization and processivity on both DNA and RNA templates, strand displacement, ribonucleotide misincorporation, and resistance to nucleoside analogs. The RT variants Tyr-115–Phe and Phe-116–Tyr are similar to wild-type HIV-1 RT in most, but not all, respects. In contrast, the RT variant Tyr-115–Val is significantly impaired in polymerase activity compared with wild-type RT; however, Tyr-115–Val is able to incorporate ribonucleotides as well as deoxyribonucleotides during polymerization and is resistant to a variety of nucleoside analogs.

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