Result: The next two most common major LPV DRMs:I50V and V82F -accounted for an additional 4% of viruses with predicted intermediate or high-level LPV resistance.
Table: I50V
The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops.
PMID: 29124158
2015
Biochemistry and biophysics reports
Introduction: Clinical isolates previously obtained from the Wayne State University Infectious Disease Clinic in Detroit, MI contain major drug resistance mutations L33F, I47V, I50V, I54M, L76V, V82I/F, and I84F as well as nonpolymorphicaccessory mutations L10V/G, V11I, I13V, K20T/R, L33I/M, K43T, F53L, A71L, T74P, and L89V.
2014 Update of the drug resistance mutations in HIV-1.
Discussion: Some of these mutations appear to have a greater effect on susceptibility than others (eg, I50V vs V11I).
Discussion: The presence of mutations L24I, I50L/V, F53Y/L/W, I54L, and L76V have been associated with improved virologic response to tipranavir in some studies.
Genotypic resistance profiles of HIV-2-treated patients in West Africa.
Method: Among the protease inhibitor resistance mutations, the I50V, I54M, and I84V were associated with resistance to darunavir.
Method: In this study, HIV-2 resistance mutations were identified using the list generated by the 'Collaborative HIV and Anti-HIV Drug Resistance Network', leading to the following mutations in reverse transcriptase - K65R, D67G/N, N69S/T, K70N/R, L74V, V111I, Y115F, M184I/V, Q151M, S215A/C/F/L/Y,
Characteristics of HIV-1 natural drug resistance-associated mutations in former paid blood donors in Henan Province, China.
Discussion: Results from the HIV-1 drug resistance mutation research by the International AIDS Society-USA (updated in March 2013) have revealed that PI resistance mutation sites are L10I, K20M, V32I, M36I, M46I/L, I47V/A, I50V, Q58E, A71V, G73S, V82A/F/T, I84V, L89V,L90M; NRTIs resistance mutations are M41L, A62V, PMID: 24629078
2014
BMC bioinformatics
Result: We modelled the proteins with unusual mutations (L5F, D29V, L63G, L63R, P79L and T91V), natural polymorphisms (L63H andL63S), and drug-resistant mutant PRs with single mutations or patterns of mutations (D30N, V32I, M36I, M46I, I47V, G48V, I50V, I50L, I54M, Q58E, T74P,
Table: I50V
Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 protease.
Abstract: To understand the molecular basis of this protease-substrate coevolution, we solved the crystal structures of drug resistant I50V/A71V HIV-1 protease with p1-p6 substrates bearing coevolved mutations.
The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics.
Introduction: The DetMDRs differ from isolates previously studied by our group in that these contain the major drug resistance mutations L33F, I47V, I50V, I54M, L76V, V82I/F, and I84F not present in the previous cohort (Table 1).
Revealing origin of decrease in potency of darunavir and amprenavir against HIV-2 relative to HIV-1 protease by molecular dynamics simulations.
Result: also proves that the mutation I50V of PR1 results in the decrease of the distance between I50'Calpha and D25'Calpha, which basically agrees with our studies here.
Cobicistat-boosted darunavir in HIV-1-infected adults: week 48 results of a Phase IIIb, open-label single-arm trial.
Method: Patients were required to have plasma VL >=1000 HIV-1 RNA copies/ml (Amplicor HIV-1 Monitor Test, version 1.5, Roche Diagnostics, Basel, Switzerland) at screening, eGFRCG >=80 ml/min, genotypic sensitivity to the two investigator-selected N[t]RTIs (GenoSure MG assay, Monogram Biosciences, South San Francisco, CA, USA), and none of the following darunavir RAMs: V11I, V32I, L33F, I47V, I50V, I54M, I54L, T74P, L76V, I84V or L89V.
HIV mutation literature information.
PMID: 
2015
PloS one
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