Mechanism of Darunavir (DRV)'s High Genetic Barrier to HIV-1 Resistance: A Key V32I Substitution in Protease Rarely Occurs, but Once It Occurs, It Predisposes HIV-1 To Develop DRV Resistance.
Introduction: (2012) compared PR1 mutants containing these three mutations (V32I, I47V, and V82I) with PR1 and PR2 wild-type structures in terms of global biochemical properties and their interactions with APV.
Introduction: Several studies have focused on the link between the differences of PR1 and PR2 affinity and certain amino acid changes (V32I, M46I, I47V, L76M, and V82I) between PR1 and PR2 binding sites.
Result: In this section, we studied the link between s
HIV-1C proviral DNA for detection of drug resistance mutations.
Result: Positions V82I (PR) and A98S (RT) were most common polymorphic alterations in both compartments (Table 5).
Temporal Patterns and Drug Resistance in CSF Viral Escape Among ART-Experienced HIV-1 Infected Adults.
PMID: 28328546
2017
Journal of acquired immune deficiency syndromes (1999)
Result: The most common PI mutations were V82A/T/F/S/I; V32I mutation was present in 3 cases, and has been associated with high level of resistance in combination with other PI mutations.
Room Temperature Neutron Crystallography of Drug Resistant HIV-1 Protease Uncovers Limitations of X-ray Structural Analysis at 100 K.
PMID: 28195728
2017
Journal of medicinal chemistry
Abstract: To better understand binding of clinical inhibitors to resistant HIV-1 protease, we used room-temperature joint X-ray/neutron (XN) crystallography to obtain an atomic-resolution structure of the protease triple mutant (V32I/I47V/V82I) in complex with amprenavir.
Introduction: In this work, we report a room temperature XN structure of the PR triple mutant variant V32I/I47V/V82I (referred to as PRTM henceforth) in complex with APV at pH 6.0 (PDB ID 5T8H), and compare it to the room temperature XN structure of PRWT-APV complex and to the low temperature PRTM-APV X-ray structure.
Method: The PRTM has substitutions V32I, PMID: 27897226
2016
Scientific reports
Discussion: For instance, V82I polymorphism in subtype G contributes to emergence of I82M/T/S resistance after protease inhibitor based treatment failure.
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.
Viral Genetic Diversity and Polymorphisms in a Cohort of HIV-1-Infected Patients Eligible for Initiation of Antiretroviral Therapy in Abuja, Nigeria.
PMID: 25582324
2015
AIDS research and human retroviruses
Abstract: Eleven polymorphic mutations (G16E, K20I, L23P, E35D, M36I, N37D/S/T, R57K, L63P, and V82I) were detected in the PR that were subtype or CRF specific while only three mutations (D123N, I135T, and I135V) were identified in the RT.
Result: Of the 271 sequences analyzed, 11 polymorphic mutations (G16E, K20I, L23P, E35D, M36I
Characterization of HIV drug resistance mutations among patients failing first-line antiretroviral therapy from a tertiary referral center in Lusaka, Zambia.
Discussion: Another Zambian study compared therapy-nave patients before (n = 30) and after (n = 66) the availability of free-of-charge ART, showing no statistically significant difference in major PI DRMs (V82I: 10% vs.
Treatment-Emergent Mutations and Resistance in HIV-Infected Children Treated with Fosamprenavir-Containing Antiretroviral Regimens.
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 mutation literature information.
PMID: 
2018
mBio
Browser Board
Co-occurred Entities
Filtrator
ViMRT