literature

HIV mutation literature information.

Interpretation of genotypic resistance to predict darunavir/ritonavir failure in antiretroviral experienced patients.

PMID: 22067663 2012 Journal of acquired immune deficiency syndromes (1999)

Abstract: Four mutations (V32I, I50V, L76V, I84V) were predictive of failure, the hazard ratio progressively increased by detecting 1 (hazard ratio: 2.0, 95% confidence interval: 1.3 to 3.0), 2 (3.6, 2.0 to 6.6), or 3 of them (9.7, 2.8 to 33.5).

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

Introduction: In the present study, we have tested the SWCNTs as inhibitors in WT as well as in three primary mutants (I50VPR, V82APR and I84VPR) of HIV-1-PR by docking the SWCNT in the active site region, and then performed all-atom molecular dynamics (MD) simulations for the complexes.

Method: The PDB entries are: 1T3R for the wild type (WT), 2F8G for the I50VPR, 2QD7 for the V82APR, and 2NNP for the I84VPR mutants.

Result: Although the WT, I50VPR, V82APR and I84VPR mutant trajectories have significant overlaps, some differences can still be observed (Figure 6a).

Genotypic resistance profiles associated with virological failure to darunavir-containing regimens: a cross-sectional analysis.

PMID: 22237471 2012 Infection

Abstract: DISCUSSION: The higher statistical difference at baseline between failing versus non-failing patients was observed for the V32I and I84V mutations.

Interaction of I50V mutant and I50L/A71V double mutant HIV-protease with inhibitor TMC114 (darunavir): molecular dynamics simulation and binding free energy studies.

PMID: 22239286 2012 The journal of physical chemistry. B

Introduction: The resistance of the inhibitor GRL-98065, an analog of TMC114 just aniline group replaced by a 1,3-benzodioxole group, to mutants I50V and V82A was attributed to a higher entropic contribution than in the wild type (WT) HIV-pr, and the reduced van der Waals may be responsible to the drug resistance of I84V to GRL-98065.

Result: For example, L90M and V82F/I84V mutations open the flap a bit more in the mutant than the WT, whereas M46I mutation makes the flap more closed.

HIV-1 protease with 20 mutations exhibits extreme resistance to clinical inhibitors through coordinated structural rearrangements.

PMID: 22404139 2012 Biochemistry

5Result: Four ""first shell"" mutations D30N, V32I, I47V and I84V alter residues making direct contacts with DRV and SQV inhibitors."

Result: First, mutation of four (D30N, V32I, I47V and I84V) of the seven residues forming the S2/S2' subsites alters their size, shape and charge.

Result: In the PR20/SQV complex, the P2' group of SQV shifts more than 1.5 A towards the shorter I84'V to compensate for the larger S2' subsite and maintain interactions with D30N, V32I, I47V and I84V (Figure 5E).

Three main mutational pathways in HIV-2 lead to high-level raltegravir and elvitegravir resistance: implications for emerging HIV-2 treatment regimens.

PMID: 23028968 2012 PloS one

Table: I84V

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

Low prevalence of transmitted drug resistance in patients newly diagnosed with HIV-1 infection in Sweden 2003-2010.

PMID: 22448246 2012 PloS one

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

Transition states of native and drug-resistant HIV-1 protease are the same.

PMID: 22493227 2012 Proc Natl Acad Sci U S A

Abstract: The KIEs measured for the native and I84V enzyme indicate nearly identical transition states, implying that a true transition-state analogue should be effective against both enzymes.

Abstract: We have measured primary (14)C and (15)N KIEs and secondary (3)H and (18)O KIEs for native and multidrug-resistant HIV-1 protease (I84V).

Abstract: We observed (14)C KIEs ((14)V/K) of 1.029 +- 0.003 and 1.025 +- 0.005, (15)N KIEs ((15)V/K) of 0.987 +- 0.004 and 0.989 +- 0.003, (18)O KIEs ((18)V/K) of 0.999 +- 0.003 and 0.993 +- 0.003, and (3)H KIEs ((3)V/K) KIEs of 0.968 +- 0.001 and 0.976 +- 0.001 for the native and I84V enzyme, respectively.

Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir.

PMID: 22350569 2012 Journal of computer-aided molecular design

Abstract: Drug resistance arises from an increase in the energetic contribution from the van der Waals interactions between APV and PR (V32I, I50V, and I84V mutant) or a rise in the energetic contribution from the electrostatic interactions between the inhibitor and its target (I54M and I54V mutant).

Abstract: However, the affinities of the drug resistant protease variants V32I, I50V, I54V, I54M, I84V and L90M to amprenavir are decreased 3 to 30-fold compared to the wild-type.

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