Genotypic changes in human immunodeficiency virus type 1 associated with loss of suppression of plasma viral RNA levels in subjects treated with ritonavir (Norvir) monotherapy.
Abstract: Ongoing viral replication in the presence of drugs resulted in the appearance of additional genotypic changes, including the L90M saquinavir resistance mutation, and decreased phenotypic susceptibility.
Human immunodeficiency virus type 1 protease genotypes and in vitro protease inhibitor susceptibilities of isolates from individuals who were switched to other protease inhibitors after long-term saquinavir treatment.
Abstract: In vitro susceptibility assays showed that all 13 isolates with reduced susceptibilities to two or more protease inhibitors had either the G48V or L90M mutation, along with an average of six other protease mutations.
Drug-resistant HIV-1 proteases identify enzyme residues important for substrate selection and catalytic rate.
Abstract: Mutants containing R8K, V32I, V82T, I84V, G48V/L90M, or V82T/I84V substitutions were analyzed for differences in substrate preference and catalytic efficiency using a set of single amino acid substituted HIV-1 CA-NCa cleavage site peptides.
Resistance mutations in protease and reverse transcriptase genes of human immunodeficiency virus type 1 isolates from patients with combination antiretroviral therapy failure.
PMID: 9780274
1998
The Journal of infectious diseases
Abstract: The most commonly observed PR mutations were L10I, V82A/T/F, and L90M.
An Escherichia coli expression assay and screen for human immunodeficiency virus protease variants with decreased susceptibility to indinavir.
PMID: 9835523
1998
Antimicrobial agents and chemotherapy
Abstract: The discovered HIV protease variants contain amino acid substitutions commonly associated with indinavir resistance in clinical isolates, including the substitutions L90M, L63P, I64V, V82A, L24I, and I54T.
Abstract: The highly sensitive system detects the contributions of single substitutions such as I84V, L90M, and L63P.
Escape mutants of HIV-1 proteinase: enzymic efficiency and susceptibility to inhibition.
Abstract: The L90M proteinase again showed only marginal changes in its susceptibility to all except one of the inhibitors examined.
Abstract: The L90M proteinase showed only small changes, whereas the activity of the other mutant enzymes was compromised more severely, particularly towards substrates of the -Aromatic * Pro- and pseudo-symmetrical types.
Abstract: The K(i) values determined for one inhibitor (Ro31-8959) showed that its potency towards the V82F, L90M, I84V and G48V mutant proteinases respectively was 2-, 3-, 17- and 27-fold less than against the wild-type proteinase.
Abstract: The proteinases containing mutations of single residues (e.g., G48V, V82F, I84V
Emergence of resistant variants of HIV in vivo during monotherapy with the proteinase inhibitor saquinavir.
PMID: 9222047
1997
The Journal of antimicrobial chemotherapy
Abstract: Hence, in vivo, the Leu90-->Met but not the Gly48-->Val mutation is necessary, but not sufficient, for phenotypic resistance to saquinavir in HIV.
Abstract: The Leu90-->Met mutation was observed in five subjects, but a greater than eight-fold phenotypic change in antiviral susceptibility was seen in only two of these.
Kinetic properties of saquinavir-resistant mutants of human immunodeficiency virus type 1 protease and their implications in drug resistance in vivo.
Abstract: Although the protease activity of G48V, L90M, and G48V/L90M are only about 10, 7, and 3% of that of the wild-type HIV-1 protease in the absence of inhibitor, the resistance tendencies of the three mutants are clearly manifest by relatively less activity loss as inhibitor concentration becomes higher.
Abstract: In order to study the basis of resistance of human immunodeficiency virus, type 1 (HIV-1), to HIV-1 protease inhibitor saquinavir, the catalytic and inhibition properties of the wild-type HIV-1 protease and three saquinavir resistant mutants, G48V, L90M, and G48V/L90M
Human immunodeficiency virus type 1 proteinase resistance to symmetric cyclic urea inhibitor analogs.
PMID: 9371337
1997
Antimicrobial agents and chemotherapy
Abstract: L90M had a lower Km than the wild type, whereas the G48V/L90M double mutant had an increased Km compared with that of the wild type, contributing to a 10-fold reduction in the k(cat)/Km.
Abstract: The proteinase gene of resistant virus was sequenced, and key mutations (G48V, V82A, I84V, L90M, and G48V/L90M) were introduced into clones used for the expression, purification, and further characterization of the enzyme.
In vivo resistance to a human immunodeficiency virus type 1 proteinase inhibitor: mutations, kinetics, and frequencies.
PMID: 8648209
1996
The Journal of infectious diseases
Abstract: A Leu90-->Met exchange was the predominant resistance mutation in vivo; Gly48-->Val or doubly mutant virus was rarely observed.
Abstract: There was a good relationship between genotypic analysis of saquinavir resistance and data from virus assays, confirming that Leu90-->Met and Gly48-->Val are the essential exchanges in the proteinase that determine loss of sensitivity to this inhibitor.
HIV mutation literature information.
PMID: 
1998
Journal of virology
Browser Board
Co-occurred Entities
Filtrator
ViMRT