The nucleoside analog-resistant E89G mutant of human immunodeficiency virus type 1 reverse transcriptase displays a broader cross-resistance that extends to nonnucleoside inhibitors.
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 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.
Kew
Y
Y
Department of Microbiology & Immunology, Albert Einstein College of Medicine Bronx, New York 10461, USA.
Salomon
H
H
Olsen
L R
LR
Wainberg
M A
MA
Prasad
V R
VR
D019380:Anti-HIV Agents / Q000494:pharmacology*; D004352:Drug Resistance, Microbial; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D054303:HIV Reverse Transcriptase / Q000037:antagonists & inhibitors* / Q000235:genetics*; D015497:HIV-1 / Q000187:drug effects* / Q000201:enzymology* / Q000235:genetics; D009154:Mutation; D009705:Nucleosides / Q000494:pharmacology*
D019380:Anti-HIV Agents; D004791:Enzyme Inhibitors; D009705:Nucleosides; D054303:HIV Reverse Transcriptase