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

Paul L. Boyer, Stefan G. Sarafianos, Edward Arnold, Stephen H. Hughes

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)3056-3061
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number7
DOIs
StatePublished - Mar 28 2000

All Science Journal Classification (ASJC) codes

  • General

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