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Antimicrobial Agents and Chemotherapy, February 1998, p. 447-452, Vol. 42, No. 2
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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
Paul L.
Boyer,
Hong-Qiang
Gao, and
Stephen H.
Hughes*
ABL-Basic Research Program, NCI-Frederick
Cancer Research and Development Center, Frederick, Maryland
21702-1201
Received 28 May 1997/Returned for modification 22 July
1997/Accepted 5 November 1997
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.
*
Corresponding author. Mailing address: NCI-FCRDC, P.O.
Box B, Bldg. 539, Frederick, MD 21702-1201. Phone: (301) 846-1619. Fax:
(301) 846-6966. E-mail: hughes{at}fcrfv1.ncifcrf.gov.
Antimicrobial Agents and Chemotherapy, February 1998, p. 447-452, Vol. 42, No. 2
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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