Introduction: reported that the protease variant with mutation sites in 80 s loops (V82F/I84V) shows more frequent and rapid flap curling than wild-type (WT) HIV-1 PR does.
HIV-1 transmitted drug resistance and genetic diversity among patients from Piaui State, Northeast Brazil.
Result: The patient met VF criteria at week 24, at which time the major viral PI treatment-emergent mutations I50I/V, I54I/M, and V82F/I were detected.
HIV Drug Resistance Surveillance in Honduras after a Decade of Widespread Antiretroviral Therapy.
Result: The next two most common major LPV DRMs:I50V and V82F -accounted for an additional 4% of viruses with predicted intermediate or high-level LPV resistance.
Table: V82F
Structural studies on molecular mechanisms of Nelfinavir resistance caused by non-active site mutation V77I in HIV-1 protease.
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.
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.
The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics.
Introduction: The DetMDRs differ from isolates previously studied by our group in that these contain the major drug resistance mutations L33F, I47V, I50V, I54M, L76V, V82I/F, and I84F not present in the previous cohort (Table 1).
The impact of active site mutations of South African HIV PR on drug resistance: Insight from molecular dynamics simulations, binding free energy and per-residue footprints.
PMID: 24267738
2014
Chemical biology & drug design
Abstract: Against the V82F/I84V variant, saquinavir, indinavir, and nelfinavir lose remarkable entropic contributions relative to both wild-type and V82A C-SA HIV PRs.
Abstract: Molecular dynamics simulations and binding free energy calculations were used to provide an understanding of the impact of active site drug-resistant mutations of the South African HIV protease subtype C (C-SA HIV PR), V82A and V82F/I84V on drug resistance.
Trends in Genotypic HIV-1 Antiretroviral Resistance between 2006 and 2012 in South African Patients Receiving First- and Second-Line Antiretroviral Treatment Regimens.