literature

HIV mutation literature information.

Unique Flap Conformation in an HIV-1 Protease with High-Level Darunavir Resistance.

PMID: 26870021 2016 Frontiers in microbiology

Result: Each rFS5929R1 virus without I47V (rFS5929R1I47) and rFS5929R1 without I50V (rFS5929R1I50) exhibited a >175-fold and 96.9-fold increase in DRV resistance, respectively, whereas the rFS5929R1 without the two mutations (rFS5929R1I47/I50) exhibited a 20.4-fold increase.

Result: Interestingly, the regions included the two major DRV resistance mutations (I47V and I50V) and one minor mutation (V32I), which were induced by the in vitro selection (Figure 3C).

Result: The major virus (referred to as FS5929R1) had two major DRV resistance mutations (I47V and I50V), four minor mutations (V11I, V32I, L33F, and L89V

HIV-1 Transmitted Drug Resistance Mutations in Newly Diagnosed Antiretroviral-Naive Patients in Turkey.

PMID: 26414663 2016 AIDS research and human retroviruses

Abstract: Nonnucleoside reverse transcriptase inhibitor-associated TDRMs were detected in 3.3% (44/1,306) of patients (L100I, K101E/P, K103N/S, V179F, Y188H/L/M, Y181I/C, and G190A/E/S) and TDRMs to protease inhibitors were detected in 2.3% (30/1,306) of patients (M46L, I50V, I54V, Q58E, L76V, V82A/C/L/T, N83D, I84V, and L90M

Treatment-Emergent Mutations and Resistance in HIV-Infected Children Treated with Fosamprenavir-Containing Antiretroviral Regimens.

PMID: 26157536 2015 The open AIDS journal

Result: At VF, the following major treatment-emergent PI mutations or mutation mixtures were detected: M46M/I, I50I/V, I54I/M/V, and I84I/V, and the virus developed FPV RS.

Result: The major PI treatment-emergent mutations selected at VF in virus from Patient-1 included M46M/L, I50I/V, I54I/L, and Q58Q/E, while virus from Patient-2 selected the V82V/A mutation.

Result: The patient met VF criteria at week 24, at which time the major viral PI treatment-emergent mutations I50I/V,

Exploring the drug resistance of V32I and M46L mutant HIV-1 protease to inhibitor TMC114: flap dynamics and binding mechanism.

PMID: 25562662 2015 Journal of molecular graphics & modelling

Introduction: It was found that, the mutations D30N and I50V results in the drug resistance to TMC114; however the changes due to mutations V82A, I84V and L90M are well adapted by TMC114.

Introduction: Our previous studies on binding Gibbs free energies for WT, I50V single mutant and I50L/A71V double mutant showed that I50V decreases the binding affinity for TMC114, while the double mutant I50L/A71V increases the binding affinity and may be well adapted to accommodate the TMC114 in the active site.

Introduction: performed MD simulation studies combined with MM-PBSA to investigate the binding energies of TMC11

Single Genome Analysis for the Detection of Linked Multiclass Drug Resistance Mutations in HIV-1-Infected Children After Failure of Protease Inhibitor-Based First-Line Therapy.

PMID: 25923117 2015 Journal of acquired immune deficiency syndromes (1999)

5Result: PI and NRTI DRMs were detected by SGS only and at baseline in

8Discussion: Furthermore, despite failing AZT and LPV/r-containing therapy, T215I and T219N in RT and I50V in PR were not detected by SGS or bulk sequencing during ART for the 2 children (""D and E"") who harbored these mutations in their baseline viral populations."

8Discussion: The baseline PI DRM I50V, TAM revertant K215I, and the TAM K219N of the double mutant Y181C + K219N that were detected in ""D, E, and J"" may have also been vertically transmitted."

Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir.

PMID: 26012849 2015 Scientific reports

Introduction: Similarly, the I50V mutation in flap regions selected by APV shows more flexible flaps, and single mutation distant from flap regions such as L63P or L10I can increase the flexibility of flap regions as well.

Discussion: The crystal structure comparison of flap variants (I50V, I54V, and I54M) bound with SQV and variants (G48V, I54V, and I54M) bound with DRV suggested that the change in polar interactions between protease and inhibitors have the best correlation with observed resistance mutations.

Genetic Characteristics of CRF01_AE Among Newly Diagnosed HIV-1-Infected 16- to 25-Year Olds in 3 Geographic Regions of Guangxi, China.

PMID: 26020400 2015 Medicine

Result: Two TDR mutations, M46I (2) and I50V (1) were found in the protease region, and the other eight TDR mutations, K65E(1), D67N(1), T69N(1), K103N(1), Y181C(2), G190E(1), L210W(1), and P225H(1) were from the reverse transcriptase fragment.

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: 26198456 2015 Journal of computational chemistry

Abstract: I50V mutation as one of the most significant mutations occurring in HIV-1 protease will be investigated in this study.

Abstract: In addition, the mechanism governing the decrease in the binding affinity of PI in the presence of I50V mutation was also explored to provide insights pertaining to the design of the next generation of anti-HIV drugs.

Abstract: Molecular dynamics (MD) simulation was utilized to examine the effect of I50V mutation on the binding of two PIs namely indinavir and amprenavir to HIV-1 protease.

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: 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).

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.

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