Drug Resistance Mutations Against Protease, Reverse Transcriptase and Integrase Inhibitors in People Living With HIV-1 Receiving Boosted Protease Inhibitors in South Africa.
Abstract: M46I and I47V were the most common mutations for Result: The most common mutations were M46I and I47V for PIs, M184V for NRTIs, and K103N/S for NNRTIs (Table 6).
Table: I47V
Discussion: M46I and I47V were the most frequent mutations for PIs; M184V was the most common mutation for the NRTIs, and K103N/S was the most common mutation for NNRTIs.
HIV-1 acquired drug resistance to integrase inhibitors in a cohort of antiretroviral therapy multi-experienced Mexican patients failing to raltegravir: a cross-sectional study.
Result: Forward transmission of SDRMs throughout the period 2014-2017 was determined in several TCs: (1) T215S (n = 20) and its sub-cluster T215S + L210W (n = 9) (2), K101E (n = 14) and (3) V32I + I47V + T215D/E + L100I + K103N (n = 8).
Result: Resistance to PIs was detected in 10/403 (2.5%) persons, most often due to mutations V32I (1.9%) and I47V (1.9%).
Result: The Croatian sequences contained the SDRM pattern PI: V32I, I47V + NRTI: T215E/D +
Structural studies of antiviral inhibitor with HIV-1 protease bearing drug resistant substitutions of V32I, I47V and V82I.
PMID: 31092330
2019
Biochemical and biophysical research communications
Abstract: This
Discussion: Overall, the loss of internal contacts among flap residues and disruption of the ion pair between Arg8 and Asp29' are consistent with molecular dynamics simulations suggesting substitutions V32I, I47V and V82I in HIV-2 PR decrease the hydrophobic interactions with APV and DRV.
Discussion: This new structure of PRTri/1 suggests how drug resistant mutations of V32I and I47V on opposite sides of the S2 and S2' subsites can partially compensate for altered hydrophobic interactions with inhibitors and other protease residues, while mutation V82I induces alternate conformations of Arg8/8' and introduces new interactions with Leu10 and the P2 group of 1.
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.
Table: I47V
Resistance profile of the HIV-1 maturation inhibitor GSK3532795 in vitro and in a clinical study.
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
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.
Discussion: In contrast, a set of data compiled for NDA21-976/S003 and NDA21-976/S004 clearly indicates that 10 amino acid substitutions including L10F, V32I, L33F, S37N, M46I, I47V, I50V, L63P, A71V, and I84V are the most prevalent (https://www.accessdata.fda.gov/drugsatfda_docs/label/2008/021976s003s004lbl.pdf).
PMID: 29461980
2018
The Journal of clinical investigation
Abstract: The modifying effect of I47V was confined to B*57:01 and was not observed for the closely related B*57:03.
Abstract: Using whole-genome sequencing of untreated B*57+ HIV-1-infected controllers and noncontrollers, we identified a single variant (rs643347A/G) encoding an isoleucine-to-valine substitution at position 47 (I47V) of the inhibitory killer cell immunoglobulin-like receptor KIR3DL1 as the only significant modifier of B*57 protection.
HIV mutation literature information.
PMID: 
2020
Frontiers in microbiology
Browser Board
Co-occurred Entities
Filtrator
ViMRT