HIV mutation literature information.


  High predictive efficacy of integrase strand transfer inhibitors in perinatally HIV-1-infected African children in therapeutic failure of first- and second-line antiretroviral drug regimens recommended by the WHO.
 PMID: 30891603       2019       The Journal of antimicrobial chemotherapy
Result: DRMs to PIs corresponded mainly to natural polymorphism in the P gene while only the major DRMs V82A/F (n = 3; 20%) and L33F (n = 1, 6.7%) could be found.


  Resistance profile of the HIV-1 maturation inhibitor GSK3532795 in vitro and in a clinical study.
 PMID: 31622432       2019       PloS one
Method: Participants with a history of genotypic/phenotypic drug resistance to protease inhibitors (PIs) or with HIV-1 genotypic drug resistance to PIs at baseline (including D30N, M46I/L, I47V/A, G48V, I50L, I54M/L, Q58E, T74P, L76V, V82A/F/L/T/S, N83D, I84V, N88S, or L90M) were excluded, despite any reported effects of PI resistance or resistance


  Switching to bictegravir/emtricitabine/tenofovir alafenamide maintained HIV-1 RNA suppression in participants with archived antiretroviral resistance including M184V/I.
 PMID: 31430369       2019       The Journal of antimicrobial chemotherapy
Method: Primary PI-R substitutions were D30N, V32I, M46I/L, I47V/A, G48V, I50V/L, I54M/L, Q58E, T74P, L76V, V82A/F/L/S/T, N83D, I84V, N88S and L90M in PR.


  HIV-1 transmission networks across Cyprus (2010-2012).
 PMID: 29684083       2018       PloS one
Result: The second study subject, also a Romanian citizen living in Cyprus, was also infected with a sub-subtype F1strain dual-class RT and PI resistant strain carrying D67N, K70R, M184V, T215F, Y181C, M46L, I54V and V82F mutations associated with drug resistance.


  [Genetic analysis of the mutations in HIV-1 infected population in Ecuador].
 PMID: 29652972       2018       Revista chilena de infectologia
Abstract: Results The most frequent mutations were M184V/I, K101E/P/H, K103N/S, D30N, M46L/I, I54L/M, V82T/F/A/S/L and L90M in adults and F77L, K103N/S, M46L/I, V82T/F/A/S/L and L90M in children.


  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.


  Week 48 resistance analysis of Elvitegravir/Cobicistat/Emtricitabine/Tenofovir DF versus Atazanavir + Ritonavir + Emtricitabine/Tenofovir DF in HIV-1 infected women (WAVES study GS-US-236-0128).
 PMID: 28891788       2017       HIV clinical trials
Method: Primary PI-R substitutions assessed were D30N, V32I, L33F, M46I/L, I47A/V, G48V, I50L/V, I54L/M, Q58E, T74P, L76V, V82A/F/L/S/T, I84V, N88S, and L90M in PR.


  Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics.
 PMID: 27992544       2016       PloS one
Result: This inactive protease with active site D25N mutation has 22 other mutations (L10I, V11I, L23I, V32I, L33F, S37N, M46I, I47V, I50V, F53L, I54V, Q58E, D60E, L63P, H69R, A71V, G73S, V77I, V82F, L89V, L90M, <


  From antiretroviral therapy access to provision of third line regimens: evidence of HIV Drug resistance mutations to first and second line regimens among Ugandan adults.
 PMID: 28010730       2016       BMC research notes
Conclusion: The observed PI resistance mutations (V82A, V82F, V82S, M46I, M46L and I54V) are clinically significant because they are associated with highest levels of phenotypic resistance and/or strongest evidence for interfering with successful PI therapy.
Table: V82F


  Unique Flap Conformation in an HIV-1 Protease with High-Level Darunavir Resistance.
 PMID: 26870021       2016       Frontiers in microbiology
Result: The major virus (referred to as FS5929R1) had two major DRV resistance mutations (I47V and I50V), four minor mutations (V11I, V32I, L33F, and L89V), and V82F.
Table: V82F
Discussion: Therefore, the curling conformation would also shield these residues, resulting in the inhibition of DRV binding to monomeric PR; in contrast, the presence of four mutations (V32I, L33F, I54V, and V82F) in FS5929R1 PR might directly impair the DRV binding to monomeric PR.



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