Method: The PR20/SQV crystal structure was solved by molecular replacement with the structure of PR mutant I50V in complex with DRV (2F8G) using MOLREP.
Low prevalence of transmitted drug resistance in patients newly diagnosed with HIV-1 infection in Sweden 2003-2010.
Method: The following resistance mutations were scored: to nucleoside reverse transcriptase inhibitors (NRTIs): M41L, K65R, D67N/G/E, T69D/insertion, K70R/E, L74V/I, V75M/T/A/S, F77L, Y115F, F116Y, Q151M, M184V/I, L210W, T215Y/F/I/S/C/D/V/E, K219Q/EN/R; to non-nucleoside revers
Transmitted drug resistance and phylogenetic relationships among acute and early HIV-1-infected individuals in New York City.
PMID: 22592583
2012
Journal of acquired immune deficiency syndromes (1999)
4Method: ARV resistance was defined by mutations at the following positions: M41L, A62V, K65R, D67N, T69ins, K70R, L74VI, Y115F, F116Y, Q151M, M184VI, T210W, T215YF and K219QE for Nucleoside Reverse Transcriptase Inhibitors (NRTI), L100I, K101EP, K103NS, V106AM
Binding of single walled carbon nanotube to WT and mutant HIV-1 proteases: analysis of flap dynamics and binding mechanism.
PMID: 23142620
2012
Journal of molecular graphics & modelling
Result: Although the WT, I50VPR, V82APR and I84VPR mutant trajectories have significant overlaps, some differences can still be observed (Figure 6a).
Result: Average distances for the WT-, I50VPR-, V82APR-, and I84VPR-SWCNT complexes are 6.55 A, 6.42 A, 6.79 A and 6.23 A, with SD 0.60 A, 0.40 A, 0.87 A and 0.35 A, respectively.
Result: Besides the mutation residue I50V/I50'V, Figure 12 and Table 3 show that Arg08 and Gly27' contributes to the binding decrease by over 1.0kcal/mol, which is basically consistent with the longer distance between the residue and the SWCNT as shown in Figures 13a.
Result: By analyzing to the distribution plot for the TriCa-B angle (Figures 8b & 8d), it observed that the I50VPR
Influence of major HIV-1 protease inhibitor resistance mutations on CTL recognition.
PMID: 21107269
2011
Journal of acquired immune deficiency syndromes (1999)
Abstract: Furthermore, M46I, I47A, and I50V could impair or abolish CTL recognition in many patients.
Abstract: Recently, we identified KMIGGIGGF (KF9) as a HLA-B*1501-restricted CTL epitope, including several major PI resistance mutations (M46I/L, I47A/V, G48V, I50V).
The L76V mutation in HIV-1 protease is potentially associated with hypersusceptibility to protease inhibitors Atazanavir and Saquinavir: is there a clinical advantage?
Abstract: The DRV-2009 score V11I+L33F+R41K+I47V+2*I50V+2*I54M+K55R+D60E+L74P+L76V+N88D+2*L89V-L10I/V-I13V-G16E-G48V-F53I/L-I62V-I66F-V77I (<0 indicating susceptibility, 0-1 intermediate resistance and >=2 resistance) correlated with VR in the derivation set (n=132, R=0.395; P<0.001).
Studies on adaptability of binding residues and flap region of TMC-114 resistance HIV-1 protease mutants.
PMID: 21696230
2011
Journal of biomolecular structure & dynamics
Abstract: We provide insight into the molecular basis of TMC-114 resistance major flap mutations (I50V and I54M) in HIV-1 protease.
TMC310911, a novel human immunodeficiency virus type 1 protease inhibitor, shows in vitro an improved resistance profile and higher genetic barrier to resistance compared with current protease inhibitors.
PMID: 21896904
2011
Antimicrobial agents and chemotherapy
Abstract: IVRS performed with r13025 in the presence of DRV required less time and resulted in more PI resistance-associated mutations (V32I, I50V, G73S, L76V, and V82I; FC in DRV EC(50) = 258).
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.
Abstract: Detailed binding free energies between TMC-114 and individual protein residues are computed by using a per-residue basis decomposition method, which provides insights into the inhibitor-protein binding mechanism and also explains the drug-resistant mechanisms of mutations D30N and I50V to TMC-114.
Abstract: In this work, molecular dynamics (MD) simulations combined with the molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) method have been performed to investigate the drug-resistant mechanisms of D30N and I50V to an inhibitor TMC-114.
Abstract: The analyses of absolute binding free energies using the separate trajectory approach suggests that the decrease in the van der Waals energy and electrostatic energy in the gas phase results in the drug resistance of D30N to TMC-114, while for
ViMRT
HIV mutation literature information.
PMID: 
2012
Biochemistry
