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

Yvonne Kew | Zendy; Horacio Salomón | Zendy; Lars Rønn Olsen | Zendy; M A Wainberg | Zendy; Vinayaka R. Prasad | Zendy

Open Access

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

Author(s) -

Yvonne Kew,

Horacio Salomón,

Lars Rønn Olsen,

M A Wainberg,

Vinayaka R. Prasad

Publication year - 1996

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.40.7.1711

Subject(s) - reverse transcriptase , nevirapine , biology , virology , reverse transcriptase inhibitor , nucleoside analogue , nucleotidyltransferase , nucleoside , virus , mutant , zidovudine , viral replication , microbiology and biotechnology , biochemistry , rna , viral disease , gene , antiretroviral therapy , viral load

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.

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