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M9480004.TXT
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1994-08-09
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Document 0004
DOCN M9480004
TI Sensitivity of (138 Glu-->Lys) mutated human immunodeficiency virus type
1 (HIV-1) reverse transcriptase (RT) to HIV-1-specific RT inhibitors.
DT 9410
AU Balzarini J; Kleim JP; Riess G; Camarasa MJ; De Clercq E; Karlsson A;
Rega Institute for Medical Research, Katholieke Universiteit; Leuven,
Belgium.
SO Biochem Biophys Res Commun. 1994 Jun 30;201(3):1305-12. Unique
Identifier : AIDSLINE MED/94296403
AB Human immunodeficiency virus type 1 (HIV-1) recombinant reverse
transcriptase (RT) containing lysine (Lys) instead of glutamic acid
(Glu) at position 138 proved fully resistant to the inhibitory effect of
TSAO derivatives, but retained marked sensitivity to all other
HIV-1-specific inhibitors investigated. In contrast, 181 Tyr-->Cys
mutated RT lost sensitivity to all HIV-1-specific inhibitors. There was
a close correlation between the sensitivity/resistance pattern of
HIV-1-specific inhibitors against mutated (138 Glu-->Lys) recombinant
HIV-1 RT and mutant virus strains selected for resistance against
TSAO-m3T in cell culture and proven to contain the 138-Lys mutation as
the sole mutation within the amino acid 50-270 region of their RT.
DE *Antiviral Agents Drug Resistance, Microbial Glutamates/CHEMISTRY
Human HIV-1/*DRUG EFFECTS/ENZYMOLOGY Mutagenesis, Site-Directed
Pyridones/PHARMACOLOGY Recombinant Proteins Reverse
Transcriptase/*ANTAGONISTS & INHIB/CHEMISTRY Structure-Activity
Relationship Support, Non-U.S. Gov't Thymidine/ANALOGS &
DERIVATIVES/CHEMISTRY/PHARMACOLOGY JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).