The nucleoside analog-resistant E89G mutant of human immunodeficiency virus type 1 reverse transcriptase displays a broader cross-resistance that extends to nonnucleoside inhibitors

Yvonne Kew, Horacio Salomon, Laurence R. Olsen, Mark A. Wainberg, Vinayaka R. Prasad

Research output: Contribution to journalArticle

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Abstract

The alteration of a glutamic acid (E) to a glycine (G) amino acid residue at position 89 (E89G alteration) in the human immunodeficiency virus type 1 reverse transcriptase confers decreased susceptibility to several nucleoside analog inhibitors. Because the nonnucleoside inhibitor-binding pocket is adjacent to the deoxynucleoside triphosphate substrate-binding site, the impact of the E89G alteration on susceptibility to nonnucleoside inhibitors was studied. Our results indicate that E89G reverse transcriptase has decreased susceptibility to TIBO R82150, nevirapine, and to a lesser extent, delavirdine. Human immunodeficiency viruses bearing the same mutation displayed decreased susceptibility to inhibition by these compounds in a cell culture virus replication assay.

Original languageEnglish (US)
Pages (from-to)1711-1714
Number of pages4
JournalAntimicrobial Agents and Chemotherapy
Volume40
Issue number7
StatePublished - Jul 1996

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R 82150
Delavirdine
Nevirapine
RNA-Directed DNA Polymerase
Virus Replication
Nucleosides
Glycine
HIV-1
Glutamic Acid
Cell Culture Techniques
Binding Sites
HIV
Amino Acids
Mutation
Human immunodeficiency virus 1 reverse transcriptase
triphosphoric acid

ASJC Scopus subject areas

  • Pharmacology (medical)

Cite this

The nucleoside analog-resistant E89G mutant of human immunodeficiency virus type 1 reverse transcriptase displays a broader cross-resistance that extends to nonnucleoside inhibitors. / Kew, Yvonne; Salomon, Horacio; Olsen, Laurence R.; Wainberg, Mark A.; Prasad, Vinayaka R.

In: Antimicrobial Agents and Chemotherapy, Vol. 40, No. 7, 07.1996, p. 1711-1714.

Research output: Contribution to journalArticle

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