HIV susceptibility to amprenavir: phenotype-based versus rules-based interpretations.
PMID: 14563897
2003
The Journal of antimicrobial chemotherapy
Abstract: Mutation I84V and accumulation of >3 PAMs were found to be associated with resistance as interpreted with all systems tested.
Abstract: Only the I84V mutation was almost invariably found in concordant resistant isolates compared with S/R isolates (60% versus 0%, respectively; P < 0.0001).
Novel enzyme-linked minisequence assay for genotypic analysis of human immunodeficiency virus type 1 drug resistance.
PMID: 14605126
2003
Journal of clinical microbiology
Abstract: ELMA is a combination of hybridization and a 1-base extension reaction, and we designed the assay to detect five mutations conferring nucleoside analogue resistance (M41L, D67N, K70R, T215Y, and M184V) and six mutations conferring protease inhibitor resistance (D30N, M46I, G48V, V82A, I84V, and L90M).
Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations.
Abstract: A mutant containing only the four active site mutations (V82A/I84V/M46I/I54V) only showed a small cooperative effect, suggesting that the mutations at the dimer interface (L10I/L90M) play a major role in eliciting a cooperative response.
Abstract: This mutant (MDR-HM) contains six amino acid mutations (L10I/M46I/I54V/V82A/I84V/L90M) located within and outside the active site of the enzyme.
Abstract: To understand the origin of resistance, three submutants containing mutations in specific regions were also studied, i.e., the active site (
Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease.
Abstract: The three-dimensional structures of indinavir and three newly synthesized indinavir analogs in complex with a multi-drug-resistant variant (L63P, V82T, I84V) of HIV-1 protease were determined to approximately 2.2 A resolution.
Emergence of resistance to protease inhibitor amprenavir in human immunodeficiency virus type 1-infected patients: selection of four alternative viral protease genotypes and influence of viral susceptibility to coadministered reverse transcriptase nucleoside inhibitors.
PMID: 11850255
2002
Antimicrobial agents and chemotherapy
Abstract: The I50V and I84V genotypes displayed the greatest reductions in susceptibility to amprenavir, although each of the amprenavir-selected genotypes conferred little or no cross-resistance to other protease inhibitors.
Abstract: These mutations fell into four distinct categories, characterized by the presence of either I50V, I54L/I54M, I84V, or V32I+I47V and often included accessory mutations, commonly M46I/L.
Evolution of primary protease inhibitor resistance mutations during protease inhibitor salvage therapy.
PMID: 11897594
2002
Antimicrobial agents and chemotherapy
Abstract: Among 78 patients meeting study selection criteria, baseline primary PI resistance mutations included L90M (42% of patients), V82A/F/T (27%), D30N (21%), G48V (6%), and I84V (4%).
Abstract: HIV-1 isolates from 38 (49%) patients failing PI salvage therapy developed new primary PI resistance mutations including L90M, I84V, V82A, and G48V.
Abstract: The persistence of L90M, V82A/F/T, G48V, and I84V during sa
Rapid and sensitive oligonucleotide ligation assay for detection of mutations in human immunodeficiency virus type 1 associated with high-level resistance to protease inhibitors.
PMID: 11923366
2002
Journal of clinical microbiology
Abstract: Oligonucleotides were designed to detect primary mutations associated with high-level resistance to amprenavir, nelfinavir, indinavir, ritonavir, saquinavir, and lopinavir, including amino acid substitutions D30N, I50V, V82A/S/T, I84V, N88D, and L90M.
Amprenavir-resistant HIV-1 exhibits lopinavir cross-resistance and reduced replication capacity.
Abstract: The order of relative replication capacity was wild-type > L10F > L10F/I84V > L10F/M46I/I50V > L10F/M46I/I47V/I50V.
Abstract: The replication capacity of viruses containing either I84V or I50V was at least 90% lower than the reference virus in the single-cycle assay.
Longitudinal use of a line probe assay for human immunodeficiency virus type 1 protease predicts phenotypic resistance and clinical progression in patients failing highly active antiretroviral therapy.
PMID: 12019110
2002
Antimicrobial agents and chemotherapy
Abstract: Combinations of protease mutations (M46I, G48V, I54V, V82A or -F, I84V, and L90M) predicted phenotypic resistance to the protease inhibitor and to nelfinavir.
Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes.
Abstract: In this paper we present a complete thermodynamic dissection of the differences between proteases from different subtypes and the effects of the V82F/I84V drug-resistant mutation within the framework of the B, C, and A subtypes.
Abstract: Relative to the wild-type B subtype protease, the V82F/I84V drug-resistant mutation within the C and A subtypes lowers the binding affinity of inhibitors by factors ranging between 40 and 3000.
HIV mutation literature information.
PMID: 
2003
The Journal of antimicrobial chemotherapy
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