A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.
PMID: 19910081
2010
European journal of medicinal chemistry
Abstract: Enthalpic and entropic balance is analyzed to explain resistance in I50V and V82A having a higher entropic contribution than in the wild type (WT) complex.
Abstract: Our results show I50V and V82A have larger structural changes than I84V compared with WT.
Abstract: The single mutations I50V, V82A and I84V are considered as the key residue mutations of the HIV-1 protease drug resistance.
HIV drug resistance surveillance using pooled pyrosequencing.
Abstract: METHODS: Recombinant viruses containing in vitro and in vivo selected I50L and I50V proteases were constructed and cultured in increasing concentrations of APV or ATV, respectively.
Abstract: RESULTS: ATV or APV alone selected I50L- or I50V-containing variants.
Abstract: Subsequent addition of ATV to I50V-containing recombinant viruses led to the reversion of this change and the later selection of I50L.
Abstract: The different pathways select for isoleucine or leucine at position 50, whereas the I50V mutation was excluded.
HIV-1 protease mutations and protease inhibitor cross-resistance.
PMID: 20660676
2010
Antimicrobial agents and chemotherapy
Abstract: Of the mutations with the greatest effect on PI susceptibility, I84AV was associated with decreased susceptibility to eight PIs; V32I, G48V, I54ALMSTV, V82F, and L90M were associated with decreased susceptibility to six to seven PIs; I47A, G48M, I50V, L76V, V82ST, and N88S were associated with decreased susceptibility to four to five PIs; and D30N, PMID: 20695887
2010
The FEBS journal
Abstract: Mutation to smaller side chains eliminated hydrophobic interactions in the PR(I50V) and PR(I54V) structures.
Abstract: The PR(I84V)-APV complex had lost hydrophobic contacts with APV, the PR(V32I)-APV complex showed increased hydrophobic contacts within t
Abstract: The observed structural changes in PR(I84V)-APV, PR(V32I)-APV and PR(I50V)-APV were related to their reduced inhibition by APV of six-, 10- and 30-fold, respectively, relative to wild-type PR.
Human immunodeficiency virus type 1 protease inhibitor drug-resistant mutants give discordant results when compared in single-cycle and multiple-cycle fitness assays.
PMID: 20826651
2010
Journal of clinical microbiology
Abstract: Five protease mutants showed statistically different fitness values by the MCA versus the SCA: the D30N, G48V, I50V, I54L, and I54M mutants.
Polymorphisms of HIV-2 integrase and selection of resistance to raltegravir.
Result: Other resistance-associated mutations present in that sample included RT mutations M184V and S215Y, and PR mutations V33I, I50V, I54M and I89V.
HIV Drug Resistance-Associated Mutations in Antiretroviral Naive HIV-1-Infected Latin American Children.
Abstract: Reverse transcriptase mutations K70R and K70E were detected in 3 and 2 subjects, respectively; protease mutation I50 V was detected in 1 subject.
Result: There were 3 different mutations detected among the 6 subjects with DRMs: reverse transcriptase mutations K70R (detected in 3 subjects), K70E (detected in 2 subjects), and protease mutation I50 V (detected in a single subject).
Distinct resistance mutation and polymorphism acquisition in HIV-1 protease of subtypes B and F1 from children and adult patients under virological failure.
PMID: 18992847
2009
Infection, genetics and evolution
Method: Mutations D30N (NFV), V32I (LPV), M46I/L (IDV/RTV), I47V/A (LPV/RTV), G48V (SQV), I50L/V (APV), V82A/F/T/S (LPV/IDV/RTV), I84V (APV/IDV/RTV) and L90M (SQV/NFV) were considered as major resistance mutations and were analyzed separately for each PI as well as quantitatively all together.
Introduction: It is, however, seen with significantly higher frequency in resistant viruses carrying the I84V mutation in PR and also specifically seen in resistant viruses carrying the I50V PR mutation, in association with L449F.
HIV mutation literature information.
PMID: 
2010
European journal of medicinal chemistry
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