literature

Detection of Gag C-terminal mutations among HIV-1 non-B subtypes in a subset of Cameroonian patients.

PMID: 35082353 2022 Scientific reports

Introduction: Following the Stanford algorithm (mutation list), minor resistance mutations (L10F, V11I, K20TV, L23I, L33F, K43T, F53L, Q58E, A71IL, G73STCA, T74P, N83D, and L89V) are assumed to have ancillary roles such as compensation for lower efficiency of proteolysis caused by major mutations; major resistance mutations (V32I, M46IL, I47VA, G48VM,

PMID: 34897227 2022 Journal of acquired immune deficiency syndromes (1999)

Table: G48V

Revealing the drug resistance mechanism of saquinavir due to G48V and V82F mutations in subtype CRF01_AE HIV-1 protease: molecular dynamics simulation and binding free energy calculations.

PMID: 34919029 2021 Journal of biomolecular structure & dynamics

Abstract: In this work, the resistance mechanism against SQV due to active site mutations G48V and V82F in CRF01_AE (AE) protease was explored.

Novel HIV PR inhibitors with C4-substituted bis-THF and bis-fluoro-benzyl target the two active site mutations of highly drug resistant mutant PR(S17).

PMID: 34111669 2021 Biochemical and biophysical research communications

Abstract: The substituted methoxy P2 group of 2 forms new interactions with G48V mutation, while the modified bis-fluoro-benzyl P1 group of 3 forms a halogen interaction with V82S mutation, contributing to improved inhibition of PRS17.

A synergy of activity, stability, and inhibitor-interaction of HIV-1 protease mutants evolved under drug-pressure.

PMID: 33314454 2021 Protein science

Abstract: A clinically-relevant, drug-resistant mutant of HIV-1 protease (PR), termed Flap+(I54V) and containing L10I, G48V, I54V and V82A mutations, is known to produce significant changes in the entropy and enthalpy balance of drug-PR interactions, compared to wild-type PR.

Abstract: To understand the molecular basis of V54A evolution, we compared nuclear magnetic resonance (NMR) spectroscopy, fluorescence spectroscopy, isothermal titration calorimetry, and enzymatic assay data from four PR proteins: PR (pWT), Flap+(I54V) , Flap+(

PMID: 34419931 2021 Journal of molecular graphics & modelling

Abstract: These results suggest that mutation G48V contributes to drug resistance by altering the conformational dynamics of the flaps.

Abstract: We have analyzed the effects of a common resistance mutation G48V in the flexible flaps of the protease by assessing the revertant PRS17V48G for changes in enzyme kinetics, inhibition, structure, and dynamics.

Correlation of HIV-1 drug resistant mutations and virologic failure.

PMID: 34584606 2021 The Pan African medical journal

Table: G48V

Prevalence of human immunodeficiency virus-1 drug-resistant mutations among adults on first- and second-line antiretroviral therapy in a resource-limited health facility in Busia County, Kenya.

PMID: 33654530 2020 The Pan African medical journal

Table: G48V

Virologic suppression in patients with a documented M184V/I mutation based on the number of active agents in the antiretroviral regimen.

PMID: 33014372 2020 SAGE open medicine

Table: G48V

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

PMID: 31920003 2020 The FEBS journal

Result: PRS17 contains a cluster of three flap mutations, M46L, G48V, and I54V, which primarily affect the conformation of the flaps.

Result: Like PRS5B, PRS17 contains only one active site mutation, V82S, which does not significantly alter the size of the inhibitor binding site or interactions with DRV relative to those of wild-type PR/DRV but may contribute to substrate recognition when combined with the G48V flap mutation.