Clinically validated mutation scores for HIV-1 resistance to fosamprenavir/ritonavir.
PMID: 18390885
2008
The Journal of antimicrobial chemotherapy
Abstract: Two fosamprenavir/ritonavir mutation scores were constructed: score A (L10F/I/V + L33F + M36I + I54L/M/V/A/T/S + I62V + V82A/F/C/G + I84V + L90M) was based only on mutations associated with a worse VR, whereas score B (L10FIV + L33F + M36I + I54L/M/V/A/T/S + A71V - V77I - N88S + L90M) also took into account favourable mutations.
Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir.
Result: The 80's loop shows intrinsic flexibility as described previously for atomic resolution structures of saquinavir complexes with wild type PR and mutants V82A and I84V and a 9X mutant with indinavir.
Structural and kinetic analysis of pyrrolidine-based inhibitors of the drug-resistant Ile84Val mutant of HIV-1 protease.
Abstract: Although the Ile50Val mutation leads to a significant decrease in affinity for all compounds in this series, they retain or even show increased affinity towards the important Ile84Val mutation.
Abstract: Herein, we report the influence of the active-site mutations Ile50Val and Ile84Val on these inhibitors by structural and kinetic analysis.
Active-site mutations in the South african human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study.
Abstract: Study of active-site mutations (the V82A single mutation and the V82F I84V double mutation) in the less-studied South African HIV type 1 subtype C (C-SA) protease indicated that neither mutation had a significant impact on the proteolytic functioning of the protease.
Abstract: Therefore, our results show that the C-SA V82F I84V double mutation decreased the binding affinities of protease inhibitors to levels significantly lower than that required for effective inhibition.
Genotypic resistance analysis of the virological response to fosamprenavir-ritonavir in protease inhibitor-experienced patients in CONTEXT and TRIAD clinical trials.
PMID: 18852278
2008
Antimicrobial agents and chemotherapy
Abstract: The JT procedure led to selecting the CONTEXT/TRIAD genotypic set of mutations, I15V, M46I/L, I54L/M/V, D60E, L63P/T, and I84V, as providing the strongest association with the VR (P = 1.45 x 10(-11)).
Transmission networks of drug resistance acquired in primary/early stage HIV infection.
Result: In addition, cluster C represents an MDR transmission network, wherein all four PHIs harboured K103N and three of the four also harboured L10I, I54V, A71V, V82A/I/T, I84I/V, and L90M.
Combating HIV resistance - focus on darunavir.
PMID: 19209258
2008
Therapeutics and clinical risk management
Abstract: Darunavir resistance-associated mutations have been defined as V11I, V32I, L33F, I47V, I50V, I54L/M, G73S, L76V, I84V, and L89V.
Comparative studies on inhibitors of HIV protease: a target for drug design.
Abstract: The HIV protease-nelfinavir complex (PDB code: 1OHR) and HIV protease V82F/I84V double mutant-tipranavir complex (PDB code: 1D4S) were used as templates for introducing mutations on the HIV protease active site.
Identification and structural characterization of I84C and I84A mutations that are associated with high-level resistance to human immunodeficiency virus protease inhibitors and impair viral replication.
PMID: 17101675
2007
Antimicrobial agents and chemotherapy
Abstract: Isolates with the I84A or I84C mutation tended to be more resistant than the isolates with the I84V mutation.
Abstract: Modeling of the structure of the mutant proteases indicated that the I84V, I84C, and I84A mutations all create unoccupied volume in the active site, with I84A introducing the greatest change in the accessible surface area from that of the wild-type structure.
Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors.
PMID: 17116674
2007
Antimicrobial agents and chemotherapy
Abstract: After 25 weeks, other cultures had developed I50V and I84V mutations.
Abstract: The acquisition of the I54M, I84V, L90M, and L99F mutations resulted in multi-PI-resistant viruses, conferring 10-fold to more than 100-fold resistance.
HIV mutation literature information.
PMID: 
2008
The Journal of antimicrobial chemotherapy
Browser Board
Co-occurred Entities
Filtrator
ViMRT