literature

HIV-1 protease mutations and protease inhibitor cross-resistance.

PMID: 20660676 2010 Antimicrobial agents and chemotherapy

Abstract: Of the mutations with the greatest effect on PI susceptibility, I84AV was associated with decreased susceptibility to eight PIs; V32I, G48V, I54ALMSTV, V82F, and L90M were associated with decreased susceptibility to six to seven PIs; I47A, G48M, I50V, L76V, V82ST, and N88S were associated with decreased susceptibility to four to five PIs; and D30N,

PMID: 21603285 2010 The open medical informatics journal

Discussion: However, comparison is difficult due to the presence of different mutations in the HIV protease (D30N versus I54V+V82A), as well as the variability inherent in experiments employing SCID-hu mice in which a chimeric organ is created by engraftment of primary human tissues.

Discussion: Nonetheless, the differences in these results may also suggest that virus containing the D30N mutation is less able to replicate in the thymus than virus containing the V82A mutation (as is suggested by our bioinformatics model).

Discussion: who found that mice infected with a virus (210P) containing protease mutation at I54V and V82A had a higher level of viremia than mice infected w

Patients with discordant responses to antiretroviral therapy have impaired killing of HIV-infected T cells.

PMID: 21124822 2010 PLoS pathogens

Abstract: In such patients, two protease mutations, I54V and V82A, occur more frequently.

Abstract: Primary CD4 T cells expressing I54V or V82A protease underwent less cell death than with WT or other mutant proteases.

Method: HIV (HXB2) viral stocks containing either the WT protease gene or mutations coding for single amino acid substitutions (I54V, V82A, or L90M) of the protease gene were produced as follows: Mutant PR coding sequences were generated from a pGEM vector containing the HIV-1 LAI (clone HXB2)

Human immunodeficiency virus type 1 protease inhibitor drug-resistant mutants give discordant results when compared in single-cycle and multiple-cycle fitness assays.

PMID: 20826651 2010 Journal of clinical microbiology

Abstract: When all the mutants were ranked in order from most to least fit for both assays, 4 protease mutants moved more than 5 positions in rank: the D30N, I54L, I54M, and V82A mutants.

Frequency and diversity of human immunodeficiency virus type 1 mutations associated with antiretroviral resistance among patients from Southern Brazil failing highly active antiretroviral therapy (HAART).

PMID: 20818500 2010 International journal of molecular medicine

Abstract: Mutations associated with resistance to protease inhibitor (PI) were detected in 124 tests (97.6%), the main ones were L90M in 28 (22.0%), V82A in 27 (21.2%), M46I in 26 (20.5%), and I54V in 23 (18.1%).

Prevalence, mutation patterns, and effects on protease inhibitor susceptibility of the L76V mutation in HIV-1 protease.

PMID: 20805393 2010 Antimicrobial agents and chemotherapy

Abstract: Common partner mutations included M46I, I54V, V82A, I84V, and L90M.

HIV drug resistance surveillance using pooled pyrosequencing.

PMID: 20174661 2010 PloS one

Table: V82A

Accurate ensemble molecular dynamics binding free energy ranking of multidrug-resistant HIV-1 proteases.

PMID: 20384328 2010 Journal of chemical information and modeling

Abstract: Multidrug resistance to lopinavir is enthalpically driven and increases through a decrease in the protein-ligand van der Waals interaction, principally due to the V82A/I84V mutation, and an increase in net electrostatic repulsion due to water-mediated disruption of protein-ligand interactions in the catalytic region.

A Comparative Molecular Dynamics, MM-PBSA and Thermodynamic Integration Study of Saquinavir Complexes with Wild-Type HIV-1 PR and L10I, G48V, L63P, A71V, G73S, V82A and I84V Single Mutants.

PMID: 20195662 2010 Journal of molecular modeling

Abstract: As a consequence, the protein-ligand contacts lost upon the V82A mutation are restored by 80s loop motions for the APV-bound, but not for the RTV-bound form.

Abstract: In the present work we investigated the structural properties of a triple mutant (I54V-V82A-L90M) and a double mutant (V82A-L90M) that both confer strong resistance to ritonavir (RTV), but not to amprenavir (APV).

Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters.

PMID: 20695887 2010 The FEBS journal

Introduction: I54V in combination with other mutations, especially V82A, decreases the susceptibility to PI therapy.