literature

HIV mutation literature information.

HIV Viral Rebound Due to a Possible Drug-Drug Interaction between Elvitegravir/Cobicistat/Emtricitabine/Tenofovir Alafenamide and Calcium-Containing Products: Report of 2 Cases.

PMID: 30798679 2019 Journal of the International Association of Providers of AIDS Care

Conclusion: The HIV genotype at this time reported the RT gene mutations M184V and L100L/F, conferring resistance to emtricitabine and lamivudine, and protease gene mutations L10V, M36I/M, K43R, L63P,

Conclusion: The genotype at this time demonstrated no reverse transcriptase (RT) gene mutations, but the following protease gene mutations: L10V, M36I, L63P, H69H/Y, A71T/A, and I93L.

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.

PMID: 29511083 2018 mBio

Table: M36I

HIV Reverse Transcriptase and Protease Genes Variability Can Be a Biomarker Associated with HIV and Hepatitis B or C Coinfection.

PMID: 29844604 2018 Scientific reports

Result: Global sequence analysis showed that the most frequent amino acid substitutions in RT were S162C (29.4%), T200A (35.3%), M184V (32.3%), L214F (67.6%), I135T (55.9%), D177E (26.5%) and E122K (44.1%), and the most in PR were V15I (41.2%), M36I (38.2%) and E35D (23.5%).

Result: On the other hand, the minor mutations to PI found were S37N (32.3%), I15V (26.5%) and M36I (23.5%).

SURVEILLANCE OF HIV-1 DRUG-RESISTANCE MUTATIONS IN THAILAND FROM 1999 TO 2014.

PMID: 29641878 2017 The Southeast Asian journal of tropical medicine and public health

Abstract: PRdrug-associated mutations (M36I/L/V, H69K/R and L89I/M/V) previously consideredas CRF01_AE polymorphisms constituted > 90% prevalence in all samples.The launch of antiretroviral treatment influenced the pattern of mutations and theUniversal Coverage Scheme also impacted the rate of development of resistancemutations on a national scale.

Upward trends of acquired drug resistances in Ethiopian HIV-1C isolates: A decade longitudinal study.

PMID: 29049402 2017 PloS one

Result: However, in the majority of the patients at all time points, several secondary mutations that may facilitate the development of PI resistance were found at higher frequency which could be naturally occurring minor mutations/polymorphic changes (positions M36I, R41K, H69K, L89M, and I93L) but their clinical significance is uncertain.

A decade of viral mutations and associated drug resistance in a population of HIV-1+ Puerto Ricans: 2002-2011.

PMID: 28493944 2017 PloS one

Result: Class 5 shows the most internal divergence with 4 mutations that peaked markedly in one year, whereas the remaining mutations are observed at uniformly low to moderate frequencies across all years, including the M36I mutation that stands out by virtue of its sustained moderate frequency level.

Discussion: Finally, M36I, a PRO mutation whose frequency remained relatively constant over the period of study, in both Puerto Rico and throughout Latin America, influences the flexibility of the protease and its complexed substrate, thereby mediating interactions linked to increased drug resistance.

Cross-sectional study of virological failure and multinucleoside reverse transcriptase inhibitor resistance at 12 months of antiretroviral therapy in Western India.

PMID: 27631260 2016 Medicine

Result: Only 1 individual had major PI resistance mutation L90M and 5 had minor PI resistance mutations L89M, V77I, L63P, H69K/R/Q, M36I, K20I/M/R/T, G16E, and L10V/I.

Unique Flap Conformation in an HIV-1 Protease with High-Level Darunavir Resistance.

PMID: 26870021 2016 Frontiers in microbiology

Table: M36I

Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature Enzyme.

PMID: 27039930 2016 Biochemistry

Result: Only five of the mutations in PR22 are identical with those in PRS17, namely, E35D, M36I, S37D, I54V, and L90M.

Result: Other mutations in this region, E35D and M36I in both mutants, and S37D in PRS17, are located in the flap hinge loop and likely contribute to altered flap conformation and dynamics.

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: Comparison of PRS17/DRV with PR20/DRV complex, which has E35D, M36I, S37N and I62V mutations, reveals that the hinge loop conformation of PR20 in subunit A is similar to PRS17 except for absence of the K20R mutation and consequent absence of the ion pair interactions observed between Arg20 and Asp35 in PRS17/DRV (Fig 3B).

Result: Comparison of the DRV-bound complexes of PRS17 and wild type PR/DRV shows a large conformational change in the hinge loop region (residues 34-42) associated with mutations E35D

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