Abstract
The potential roles of an amino acid deletion at codon 67 (Delta67) and a Thr-to-Gly change at codon 69 (T69G) in the reverse transcriptase of human immunodeficiency virus (HIV) type 1 in drug sensitivity and relative replication fitness were studied. Our results suggest that the Delta67 and T69G changes can be categorized as mutations associated with multidrug resistance. The combination of both mutations with an L74I change (Delta67+T69G/L74I) leads to a novel 3'-azido-3'-deoxythymidine resistance motif and compensates for impaired HIV replication.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Substitution / genetics*
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Anti-HIV Agents / pharmacology
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Codon / genetics*
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Drug Resistance, Microbial / genetics*
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Drug Resistance, Multiple / genetics
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Genetic Variation / genetics
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Glycine / genetics
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Glycine / metabolism
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HIV Reverse Transcriptase / chemistry
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HIV Reverse Transcriptase / genetics*
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HIV Reverse Transcriptase / metabolism
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HIV-1 / drug effects
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HIV-1 / enzymology*
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HIV-1 / genetics
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HIV-1 / physiology
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Humans
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Inhibitory Concentration 50
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Reverse Transcriptase Inhibitors / pharmacology
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Sequence Deletion / genetics*
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Threonine / genetics
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Threonine / metabolism
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Tumor Cells, Cultured
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Virus Replication / drug effects
Substances
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Anti-HIV Agents
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Codon
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Reverse Transcriptase Inhibitors
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Threonine
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HIV Reverse Transcriptase
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Glycine