literature

HIV mutation literature information.

Drug Resistance Mutations Against Protease, Reverse Transcriptase and Integrase Inhibitors in People Living With HIV-1 Receiving Boosted Protease Inhibitors in South Africa.

PMID: 32265875 2020 Frontiers in microbiology

Result: The most common major PI RAMs observed were M46I and V82A (n = 12; 12%); I54V (n = 10; 10%); I84V and L76V (n = 7; 7%); I47A/V (n = 3; 3%); I50L/V (n = 2; 2%); and V32I (n = 2; 2%) (Table 1).

Table: V32I

Discussion: The group receiving AZT plus 3TC or ABC plus 3TC showed the highest rate of PIs such as I54V, I84V, L76V, I47A/V, I50L/V, and V32I.

HIV-1 reverse transcriptase and protease mutations for drug-resistance detection among treatment-experienced and naive HIV-infected individuals.

PMID: 32119691 2020 PloS one

Table: V32I

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.

PMID: 32041622 2020 AIDS research and therapy

Table: V32I

Highly drug-resistant HIV-1 protease reveals decreased intra-subunit interactions due to clusters of mutations.

PMID: 31920003 2020 The FEBS journal

Result: PR20 shows an expanded inhibitor binding cavity due to a cluster of mutations (D30N, V32I, I47V, and I84V).

Result: Another study on single mutants V32I, L33F, L76V, and L90M showed how remote mutations can impact inhibitor binding by altering protein ensemble dynamics through a rearranged network of residues circulating to the active site.

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: V32I

Trends in the Molecular Epidemiology and Genetic Mechanisms of Transmitted Human Immunodeficiency Virus Type 1 Drug Resistance in a Large US Clinic Population.

PMID: 29846534 2019 Clinical infectious diseases

Result: The next most common SDRMs, V32I, I50V/L, L76V, and I84V, each occurred in <=5 individuals.

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

Method: The cl

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.

Raltegravir-Induced Adaptations of the HIV-1 Integrase: Analysis of Structure, Variability, and Mutation Co-occurrence.

PMID: 31551948 2019 Frontiers in microbiology

Table: V32I

Analysis of HIV-1 diversity, primary drug resistance and transmission networks in Croatia.

PMID: 31754119 2019 Scientific reports

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 + NNRTI: L100I, K103N.

Table: V32I

Structural studies of antiviral inhibitor with HIV-1 protease bearing drug resistant substitutions of V32I, I47V and V82I.

PMID: 29511083 2018 mBio

Abstract: Compared to rHIVWT, rHIVV32I was highly susceptible to DRV and had significantly reduced fitness, explaining why V32I did not emerge upon selection of rHIVWT with DRV.

Abstract: Here, we show that the preexistence of certain single amino acid substitutions such as V32I, I54M, A71V, and I84V in HIV-1 protease facilitates the development of high-level DRV resistance.

Abstract: However, wild-type HIVNL4-3 (rHIVWT) failed to acquire V32I and did not develop DRV resistance.

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