A Mutation at Position 190 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Interacts with Mutations at Positions 74 and 75 via the Template Primer | Zendy

Paul L. Boyer | Zendy; Hongqiang Gao | Zendy; Stephen H. Hughes | Zendy

Open Access

A Mutation at Position 190 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Interacts with Mutations at Positions 74 and 75 via the Template Primer

Author(s) -

Paul L. Boyer,

Hongqiang Gao,

Stephen H. Hughes

Publication year - 1998

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.42.2.447

Subject(s) - reverse transcriptase , mutation , primer (cosmetics) , biology , polymerase , virology , virus , microbiology and biotechnology , wild type , nucleotidyltransferase , point mutation , resistance mutation , genetics , polymerase chain reaction , dna , gene , rna , chemistry , mutant , organic chemistry

We have analyzed amino acid substitutions at position G190 in the reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1). The mutation G190E, which is responsible for resistance to certain nonnucleoside inhibitors, results in RT that has significantly less polymerase activity and that is less processive than wild-type RT. Its kinetic profile with respect to dGTP and poly(rC) · oligo(dG) is significantly altered compared to that of wild-type RT. The combination of either of the mutations L74V or V75I with the G190E mutation appears to be compensatory and mitigates many of the deleterious effects of the G190E mutation.

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