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 language||English (US)|
|Number of pages||4|
|Journal||Antimicrobial agents and chemotherapy|
|Publication status||Published - Jul 1 1996|
ASJC Scopus subject areas
- Pharmacology (medical)
- Infectious Diseases