Abstract: A major natural polymorphism of the HIV-1 protease, L63P, compensated well for the impairment of fitness caused by L90M but only slightly improved the fitness of D30N.
Abstract: A nelfinavir-selected protease D30N substitution substantially decreased replicative capacity relative to WT, while a saquinavir-selected L90M substitution moderately decreased fitness.
Abstract: The D30N mutant virus was also outcompeted by the L90M mutant in the absence of drugs.
Abstract: These results indicate that the mutations which are usually initially selected by nelfinavir and saquinavir, D30N and L90M
Clinical cross-resistance between the HIV-1 protease inhibitors saquinavir and indinavir and correlations with genotypic mutations.
Abstract: Six of the patients had developed five or more mutations: L90M in two, G48V in four (of which three also contained L101), and V82A in three.
Clinical resistance patterns and responses to two sequential protease inhibitor regimens in saquinavir and reverse transcriptase inhibitor-experienced persons.
PMID: 10228055
1999
The Journal of infectious diseases
Abstract: Rapid failure was surprisingly associated with baseline presence of protease gene mutation L90M (P=.04) in the absence of D30N and with RT mutations D67N (P<.01), K70R/S (P=.02), and K219Q/W/R/E (P<.01).
Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.
PMID: 10429209
1999
European journal of biochemistry
Abstract: Mutant V82S is the least active (2-20% of wild-type protease), mutants N88D, R8Q, and L90M exhibit activities ranging from 20 to 40% and G48V from 50 to 80% of the wild-type activity.
Abstract: Mutants of HIV-1 protease that are commonly selected on exposure to different drugs, V82S, G48V, N88D and L90M, showed reduced catalytic activity compared to the wild-type protease on cleavage site peptides, CA-p2, p6pol-PR and PR-RT, c
Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH.
Abstract: Sedimentation equilibrium studies were also carried out on several drug-resistant HIV-1 protease mutants: V82F, V82F/I84V, V82T/I84V, and L90M.
Transmission of antiretroviral-drug-resistant HIV-1 variants.
Abstract: Primary-resistance mutations associated with protease inhibitors (V82A, L90M) were detected in three (4%) of 70 individuals; two of these had also RTI-resistance mutations.
The rabbit study: ritonavir and saquinavir in combination in saquinavir-experienced and previously untreated patients.
PMID: 10480631
1999
AIDS research and human retroviruses
Abstract: In this study, both phenotypic resistance to ritonavir and presence of the L90M mutation predicted the viral load response to ritonavir-saquinavir.
Abstract: There was strong correlation between phenotypic resistance to RIT and the presence of the L90M mutation.
Reduced antiretroviral drug susceptibility among patients with primary HIV infection.
Abstract: Population-based sequence analysis of these 3 samples identified multidrug-resistance mutations in reverse transcriptase (M184V, T215Y, K219K/R) and protease (L101/V, K20R, M361, M46I, G48V, L63P, A71T, V771, V82T, 184V, L90M) in the 2 latter patient samples, along with numerous polymorphisms.
Genetic variation and susceptibilities to protease inhibitors among subtype B and F isolates in Brazil.
PMID: 9925514
1999
Antimicrobial agents and chemotherapy
Abstract: The frequency of critical PI resistance substitutions (amino acid changes D30N, V82A/F/T, I84V, N88D, and L90M) among Brazilian isolates is very low (mean, 2.5%), and the associated secondary substitutions (amino acid positions 10L, 20K, 36M, 46M, 48G, 54I, 63P, 71A, and 77A) are infrequent.
HIV mutation literature information.
PMID: 
2000
International journal of antimicrobial agents
Browser Board
Co-occurred Entities
Filtrator
ViMRT