Journal
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Volume 36, Issue 9, Pages 1716-1734Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2004.02.025
Keywords
HIV-1; reverse transcriptase; nucleoside-analog resistance; fidelity; mutation rates
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Funding
- NIAID NIH HHS [R01-AI30861] Funding Source: Medline
- NIGMS NIH HHS [T32-GM07491] Funding Source: Medline
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Nucleoside-analog inhibitors of human immunodeficiency virus type I (HIV-1) reverse transcriptase (RT) were the first drugs used against the virus. It is Iona known that monotherapy with these and other drugs leads to the rapid development of viral resistance and it is being increasingly appreciated that a significant percentage of individuals receiving highly active antiretroviral therapy (HAART) also develop resistance. Considering the I-act that RT is responsible both for optimal rate of replication and an accurate copying of the viral genome, the consequence of drug-resistance mutations in RT to the biochemistry of this enzyme and to the biology of the virus are critically important. The biochemistry of HIV-1 reverse transcriptase variants harboring nucleoside-analog resistance mutations has been studied extensively. In this review, we describe a number of studies into the polymerase fidelity of nucleoside-analog resistant HIV-1 reverse transcriptase as well as the mutation rate of HIV-1 harboring these mutations. (C) 2004 Elsevier Ltd. All rights reserved.
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