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M9630211.TXT
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1996-02-27
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Document 0211
DOCN M9630211
TI Clinical isolates of HIV-1 contain few pre-existing proteinase inhibitor
resistance-conferring mutations.
DT 9603
AU Yamaguchi K; Byrn RA; Division of Hematology/Oncology, Deaconess
Hospital, Harvard; Medical School, Boston, MA 02215, USA.
SO Biochim Biophys Acta. 1995 Dec 6;1253(2):136-40. Unique Identifier :
AIDSLINE +
AB Proteinase inhibitors are an important new class of antiviral agents for
AIDS, however, in vitro experiments have identified proteinase mutations
that confer resistance to several different families of the inhibitors.
This study was undertaken to determine if these resistance-conferring
amino-acid substitutions occur in HIV strains before the application of
selective pressure. We determined the nucleic acid sequence of the
proteinase gene from the 23 clinical isolates of HIV-1 and three
laboratory-adapted strains using a method that detects the majority
species present in viral populations. Analysis of minor subpopulations
will require alternative strategies. The clinical isolates studied
contained an average of 3 (range 1-8) amino-acid substitutions as
compared to the prototypical BH10 sequence. We did not detect
substitutions characteristic of reported highly proteinase-resistant
strains. These results suggest significant variation occurs in the HIV-1
proteinase gene but pre-existing highly proteinase-resistant strains are
uncommon.
DE Amino Acid Sequence Base Sequence Comparative Study Drug Resistance,
Microbial/GENETICS Human HIV Protease/*GENETICS HIV Protease
Inhibitors/*PHARMACOLOGY HIV Seropositivity HIV-1/ENZYMOLOGY/*GENETICS
Molecular Sequence Data *Mutation Polymerase Chain Reaction Sequence
Analysis, DNA/METHODS Sequence Homology, Amino Acid Support, Non-U.S.
Gov't Support, U.S. Gov't, Non-P.H.S. Support, U.S. Gov't, P.H.S.
JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).