Introduction: L23I, D30N, E35G, M46I/L/V, G48V, I54L, G73S/T/C/A, T74S, V82A/F/S/T, I84V, N88D/S and L90M are other mutations correlated to NFV resistance.
Introduction: The other mutations which were co-occurring with DBM and TPM included major mutations like- M46IL, I54MV, I84V, L90M, N88S, V32I, G48V and V82F mutations in subtype CRF01_AE HIV-1 protease: molecular dynamics simulation and binding free energy calculations.
PMID: 26317593
2015
Journal of chemical information and modeling
Abstract: Drug resistance of mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 protease (PR) was found in clinical treatment of HIV patients with the drug amprenavir (APV).
Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir.
Introduction: Kinetic experiments show that the L90M, G48V, and L90M/G48V variants could reduce the binding affinity of inhibitors, which is caused by an increase in dissociation rates.
Introduction: indicated that the small structure difference of APV and DRV inhibitors lead to apparently different binding affinities towards WT HIV-1 PR and its two multi-drug-resistant (MDR) variants, namely Flap+ (L10I/G48V/I54V/V82A) and Act (V82T/I84V).
Discussion: The crystal structure comparison of flap variants (I50V, I54V, and
Defective hydrophobic sliding mechanism and active site expansion in HIV-1 protease drug resistant variant Gly48Thr/Leu89Met: mechanisms for the loss of saquinavir binding potency.
Introduction: Gly48Val, a primary mutation, occurs in response to SQV treatment and less often from IDV and LPV treatment- and confers high-level resistance to SQV, intermediate-level resistance to ATV, and low-level resistance to NFV, IDV, and LPV.- Gly48Met occurs in patients who ha
Discussion: In Gly48Val, loss of SQV binding is attributed to the loss of a hydrogen bond between the carbonyl oxygen of 48 and the amide of SQV.
Discussion: It is not difficult to conceive that PRG48T/L89M exhibits decreased susceptibility to SQV given that HIV-1 PR mutants containing Gly48Val or Gly48Val/Leu90Met demonstrate 13.5- and 419-fold reductions of susceptibility to SQV, respectively.
Modulation of HIV protease flexibility by the T80N mutation.
Result: Classifying the HIVp samples by the parameters c and e, the T80N mutant clusters with the inhibitor-bound forms rather than the functional apo forms of WT and G48V L63P (Fig 5).
Result: Solution scattering data were collected from a series of HIVp variants which included: WT, T80N, and the flap variant G48V that included the secondary mutation L63P.
Result: The addition of pepstatin inhibitor to either WT or the G48V/L63P mutant results in a large reduction in the flexibility of these proteins such that they approach the reduced levels of motion observed for the T80N mutant.
Result: Vector-length convolution calculations were carried out to fit WAXS patter
Natural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.
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, L76V, V82A
Genotypic resistance profiles of HIV-2-treated patients in West Africa.
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, K223R; and in protease - V47A, G48V, I50V, I54L/M,
Systematic molecular dynamics, MM-PBSA, and ab initio approaches to the saquinavir resistance mechanism in HIV-1 PR due to 11 double and multiple mutations.
PMID: 25036111
2014
The journal of physical chemistry. B
Abstract: Furthermore, it was observed that mutation accumulation may induce stabilization to SQV and to the flaps through enhanced HB interactions that lead to improved inhibition (e.g., accumulation of mutations in complexes containing L10I, G48V, L63P, I84V, or L90M single mutations).
Abstract: Herein, we extend our analysis, which includes seven double (G48V-V82A, L10I-G48V, G48V-L90M, I84V-L90M, L10I-V82A, L10I-L6
Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 Protease.
PMID: 25136270
2014
Journal of chemical theory and computation
Abstract: Flap+ is a multidrug-resistant variant of HIV-1 protease with a combination of primary and secondary resistance mutations (L10I, G48V, I54V, V82A) and a strikingly altered thermodynamic profile for darunavir (DRV) binding relative to the wild-type protease.
Introduction: This variant Flap+ (L10I/G48V/I54V/V82A) was derived as a combination of mutations that simultaneously occur in patient sequences.
Revealing origin of decrease in potency of darunavir and amprenavir against HIV-2 relative to HIV-1 protease by molecular dynamics simulations.
Result: Mutations that confer major resistance in PR1, such as G48V, L63P and I84V weaken or do not present these interactions, which basically agrees with our studies here.
HIV mutation literature information.
PMID: 
2015
BMC bioinformatics
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