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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-7-22
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pubmed:abstractText |
Serial passage of HIV-1 in CEM or MT-4 cell cultures in the presence of different HIV-1-specific reverse transcriptase (RT) inhibitors yielded mutant viruses which were resistant (i.e., 200- to 1000-fold less sensitive) to the homologous compounds. The RT of these mutant HIV-1 strains showed different amino acid substitutions depending on the class of the HIV-1-specific RT inhibitors. The following amino acid substitutions were found: 138 Glu-->Lys (TSAO-T), 181 Tyr-->Cys (nevirapine), 181 Tyr-->Cys (pyridinone), and 100 Leu-->Ile (TIBO R82150). Four TIBO (R82913)-resistant HIV-1 strains contained different amino acid substitutions: 103 Lys-->Asn (strain 2), 100 Leu-->Ile and 138 Glu-->Lys (strain B02), 100 Leu-->Ile and 181 Tyr-->Cys (strain 1), 100 Leu-->Ile and 188 Tyr-->His (strain B22). The level of cross-resistance (or sensitivity) highly depends on the nature of the amino acid substitutions. As a rule, the TSAO-resistant HIV-1 strains (138 Glu-->Lys) and TIBO (R82150 or R82913)-resistant HIV-1 strains (Leu 100-->Ile or 103 Lys-->Asn) are sensitive to the other HIV-1-specific RT inhibitors, whereas the amino acid change 181 Tyr-->Cys results in a significant reduction of sensitivity to all classes of the HIV-1-specific RT inhibitors.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HIV Reverse Transcriptase,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Reverse Transcriptase Inhibitors
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
192
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
246-53
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7685964-Amino Acid Sequence,
pubmed-meshheading:7685964-Base Sequence,
pubmed-meshheading:7685964-Genes, pol,
pubmed-meshheading:7685964-HIV Reverse Transcriptase,
pubmed-meshheading:7685964-HIV-1,
pubmed-meshheading:7685964-Molecular Sequence Data,
pubmed-meshheading:7685964-Mutation,
pubmed-meshheading:7685964-Oligodeoxyribonucleotides,
pubmed-meshheading:7685964-RNA-Directed DNA Polymerase,
pubmed-meshheading:7685964-Reverse Transcriptase Inhibitors,
pubmed-meshheading:7685964-Structure-Activity Relationship,
pubmed-meshheading:7685964-Virus Replication
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pubmed:year |
1993
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pubmed:articleTitle |
HIV-1-specific reverse transcriptase inhibitors show differential activity against HIV-1 mutant strains containing different amino acid substitutions in the reverse transcriptase.
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pubmed:affiliation |
Rega Institute for Medical Research, K. U. Leuven, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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