literature

HIV mutation literature information.

Multiple Molecular Dynamics Simulations and Free-Energy Predictions Uncover the Susceptibility of Variants of HIV-1 Protease against Inhibitors Darunavir and KNI-1657.

PMID: 34851643 2021 Langmuir

Abstract: Focused on the complexes of wild type (WT) PR and two mutant PRs (V32I/L33F/I54M/V82I and V32I/L33F/I54M/I84 V) with inhibitors Darunavir (DRV) and KNI-1657 (KNI), respectively, we have conducted research on the conformational dynamics and the resistance mechanism caused by residue mutations through multiple molecular dynamics (MD) simulations combined with an energy (MM-PBSA and solvated interaction energy (SIE)) prediction.

HIV-1 Gag mutations alone are sufficient to reduce darunavir susceptibility during virological failure to boosted PI therapy.

PMID: 32556165 2020 The Journal of antimicrobial chemotherapy

Table: V82I

HIV-1 Drug Resistance, Distribution of Subtypes, and Drug Resistance-Associated Mutations in Virologic Failure Individuals in Chengdu, Southwest China, 2014-2016.

PMID: 32280691 2020 BioMed research international

Discussion: In this study, among the PI-associated DR mutations detected, K20I/R and T74S were mainly found in CRF01_AE while A71I/T/V, Q58E, and V82I were frequently observed in CRF07_BC, indicating that the presence of different mutations may vary among different subtypes.

Polymorphisms and drug resistance analysis of HIV-1 isolates from patients on first line antiretroviral therapy (ART) in South-eastern Nigeria.

PMID: 32267869 2020 PloS one

Abstract: Other polymorphisms found include; I13V/A, E35Q, M36I/L, N37D/S/E/H, R57K/G, L63T/P/S/Q, C67E/S, H69K/R, K70R, V82I and L89M in the range of 28.6% to 100% among the different subtypes.

Result: Furthermore, a polymorphism at a known primary mutation site (V82I) was found in all subtype G/UG samples.

Result: It is important to note that C67E/S, V82I and E35Q mutations were found only among the G/UG isolat

Survey of Pretreatment HIV Drug Resistance and Genetic Transmission Network Analysis Among HIV Patients in a High Drug-Use Area of Southwest China.

PMID: 31778107 2019 Current HIV research

Result: In addition, 8 PI mutations were identified, of which the most common were I54V (1.5%) and V82A/I (1.5%), which can lead to resistance to darunavir (DRV), lopinavir (LPV) and atazanavir (ATV).

Structural Adaptation of Darunavir Analogues against Primary Mutations in HIV-1 Protease.

PMID: 30543749 2019 ACS infectious diseases

Introduction: The hydrophobic residues I84, V82 and I50 that form the S1' pocket where the P1' moiety binds [Figure 1] (as well as the S1 pocket, as the protease is a homodimer) are all highly variable, and mutations are implicated in many instances of drug resistance, commonly mutating to I84V, V82I, and I50V in multi-mutant protease variants.

Method: In short, the protease variant genes (I50V, V82I, I84V) were constructed using QuikChange site-directed mutagenesis (Genewiz) onto NL4-3 WT protease on a pET11a plasmid with codon optimization for protein expression in Escherichia coli.

Result: All three protease

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: Instead, the basic amine at P2 of inhibitor together with mutation V82I induces two alternate conformations for the side chain of Arg8 with new interactions with inhibitor and Leu10.

Abstract: This study examines the effects of four investigational inhibitors against HIV-1 protease with drug resistant mutations of V32I, I47V and V82I (PRTri) that model the inhibitor-binding site of HIV-2 protease.

Introduction: HIV-1 PR with drug resistant mutations V32I, I47V and V82I (PRTri) has been evaluated as a model for inhibition of HIV-2 PR to overcome the problem of autoproteolysis of HIV-2

PMID: 31651864 2019 Medicine

Result: The most common PI-related mutations were K20I/R (18/372, 4.84%) and V82I (13/372, 3.49%) (Table 3).

Highly Drug-Resistant HIV-1 Protease Mutant PRS17 Shows Enhanced Binding to Substrate Analogues.

PMID: 31172041 2019 ACS omega

Result: The co-occurrence of flap mutations like G48V that block P3 substrate-binding site and large substitutions at residue 82 like V82F, V82L, and V82I that block the alternate P3 binding site are expected to be detrimental to PR activity.

Discussion: However, in the presence of G48V flap mutation, mutations of residue 82 to larger side chains like V82F, V82L, and V82I may interfere with the binding of substrates, while smaller V82S and V82A mutations might play a vital role in both enhanced binding of substrate and increased resistance to PIs through the structural shift of 80'

Exploration of the effect of sequence variations located inside the binding pocket of HIV-1 and HIV-2 proteases.

PMID: 29636521 2018 Scientific reports

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

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