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 HIV mutation literature information.


  Reduced sensitivity to saquinavir: an update on genotyping from phase I/II trials.
 PMID: 8721556       1996       Antiviral research
Abstract: Genotypic resistance was defined by the Gly48-->Val and Leu90-->Met exchanges.


  Emergence of protease inhibitor resistance mutations in human immunodeficiency virus type 1 isolates from patients and rapid screening procedure for their detection.
 PMID: 8913459       1996       Antimicrobial agents and chemotherapy
Abstract: Patient human immunodeficiency virus type 1 (HIV-1) isolates that are resistant to protease inhibitors may contain amino acid substitutions L10I/V, M46L/I, G-48V, L63P, V82A/F/T, I84V, and L90M in the protease gene.


  Human immunodeficiency virus. Mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex.
 PMID: 8969180       1996       The Journal of biological chemistry
Abstract: L90M, G48V, and L90M/G48V proteases have 1/20, 1/160, and 1/1000 the affinity for saquinavir compared to
Abstract: In contrast, G48V and L90M/G48V proteases had catalytic efficiency (kcat/Km) values with TLNF-PISP, RKIL-FLDG, and AETF-YVDG that were 1/10 to 1/20 the value of WT protease.
Abstract: In contrast, the dissociation rate constants for WT, L90M, G48V, and L90M/G48V proteases complexed with saquinavir were 0.0014, 0.019, 0.128, and 0.


  Rational approaches to resistance: using saquinavir.
 PMID: 8970671       1996       AIDS (London, England)
Abstract: L90M is the predominant mutation in vivo.
Abstract: RESISTANCE TO SAQUINAVIR: Resistance to saquinavir in vitro and in vivo is associated with mutations L90M and G48V in HIV protease.


  Resistance of HIV type 1 to proteinase inhibitor Ro 31-8959.
 PMID: 7576926       1995       AIDS research and human retroviruses
Abstract: Molecular analysis of the mutations underlying resistance revealed a multistep mechanism in which an amino acid exchange was common to all resistant isolates, and in all experiments preceded further exchanges at position 90 (leucine to methionine) and/or at position 54 (isoleucine to valine).


  Analysis of resistance to human immunodeficiency virus type 1 protease inhibitors by using matched bacterial expression and proviral infection vectors.
 PMID: 7636988       1995       Journal of virology
Abstract: G48V, L90M, and G48V/L90M exhibited successively less processing in vitro than the wild-type enzyme, and the purified enzymes were 220-, 20-, and 720-fold, respectively, less sensitive to Ro 31-8959.
Abstract: The reduced enzyme sensitivity correlated directly with the sensitivities of the matched recombinant viruses, in that individual mutations L90M and G48V conferred 2-fold and 4- to 6-fold increases in 50% inhibitory concentration, respectively, whereas G48V/L90M was 8 to 10 times less sensitive to Ro 31-8959.
Abstract: The utility of this vector system was demonstrated by using protease variants glycine to valine at amino acid 48


  Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959.
 PMID: 7831807       1995       Virology
Abstract: Sequence comparison to wild-type (wt) proteinase demonstrated two amino acid substitutions in the resistant virus, a Gly to Val exchange at position 48 and a Leu to Met exchange at position 90.



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