HIV mutation literature information.


  Short Communication: Integrase Strand Transfer Inhibitors Drug Resistance Mutations in Puerto Rico HIV-Positive Individuals.
 PMID: 33800269       2021       International journal of environmental research and public health
Abstract: We identified the Q148HKR, G140S, Y143R, N155H, S147G, and E138EA major drug resistance mutations and the D232DN, T97TA, E157Q, G163GART accessory mutations.
Result: Interestingly, two samples, one collected in 2013 and the other in 2016, presented concurrently the mutations E138A, Discussion: However, the presence of three mutations (G140S, Q148H, and S147G) pose a higher risk of failing second-generation drugs.


  HIV-1 Subtype C Drug Resistance Mutations in Heavily Treated Patients Failing Integrase Strand Transfer Inhibitor-Based Regimens in Botswana.
 PMID: 33807382       2021       Viruses
Method: The mutations of interest included: T66A/I/K, E92Q, G118R, E138K/A/T, G140S/A/C, Y143R/C/H, S147G, Q148H/R/K, N155H and R263K.
Discussion: It was recently shown that it is only upon the development of the T97A mutation that variants harboring Q148H and G140S Integrase mutations started to have increased VLs.


  Interaction analysis of statistically enriched mutations identified in Cameroon recombinant subtype CRF02_AG that can influence the development of Dolutegravir drug resistance mutations.
 PMID: 33892628       2021       BMC infectious diseases
Introduction: Mutations that confer resistance to INSTIs (for example G140S, Q148H and N155H) have been structurally mapped in close proximity to the IN catalytic active site.


  HIV Pretreatment Drug Resistance Trends in Mexico City, 2017-2020.
 PMID: 34959542       2021       Pathogens (Basel, Switzerland)
Result: Resistance in IN was mainly due to R263K (1.6%) and E138AKT, G140ACS, Q148HKR (0.8% each) (Figure 6c).


  Cellular Immune Response Induced by DNA Immunization of Mice with Drug Resistant Integrases of HIV-1 Clade A Offers Partial Protection against Growth and Metastatic Activity of Integrase-Expressing Adenocarcinoma Cells.
 PMID: 34199989       2021       Microorganisms
Method: Raltegravir-resistant IN_a variants with two patterns of primary resistance to RAL: L74M, E92Q, V151I, N155H, G163R (IN_a_r1) and E138K, G140S, Q148K (IN_a_r2), and their variants inactivated by mutation D64V (IN_in_r1 and IN_in_r2) were generated by site-directed mutagenesis of pETIN_a using the QuikChange II Site-Directed Mutagenesis kit (Agilent Technologies, Santa Clara, CA, USA) with generation of plasmids pETIN_a_r1, pETIN_a_r2, pETIN_in_r1, and pETIN_in_r2, respectively.
Discussion: We synthesized an expression optimized gene encoding consensus integrase (IN


  Virologic outcomes of switching to dolutegravir functional mono- or dual therapy with a non-cytosine nucleoside analog: a retrospective study of treatment-experienced, patients living with HIV.
 PMID: 33941212       2021       AIDS research and therapy
Method: Patients with the following baseline mutations associated with reduced susceptibility to DTG: T66K, E92Q, G118R, E138 K/A/T, G140 S/A/C, Q148 H/R/K, N155H and R263K were excluded.


  Occurrence of the S230R integrase strand inhibitor mutation in a treatment-naive individual case report.
 PMID: 32629687       2020       Medicine
Discussion: Common INSTI RAMS include R263K, Q148H/R/K, G118R, G140A/S/C, E138A/K/T, N155H, and Y143C/R.


  Expanded Spectrum of Antiretroviral-Selected Mutations in Human Immunodeficiency Virus Type 2.
 PMID: 31965175       2020       The Journal of infectious diseases
Abstract: In IN, 11 nonpolymorphic TSMs occurred in >=4 persons: Q91R, E92AQ, T97A, G140S, Y143G, Q148R, A153G, N155H, H156R, R231 5-amino acid insertions.


  Structural basis of second-generation HIV integrase inhibitor action and viral resistance.
 PMID: 32001525       2020       Science (New York, N.Y.)
Abstract: Glutamine-148 histidine (Q148H) and glycine-140 serine (G140S) amino acid substitutions in integrase that result in clinical INSTI failure perturb optimal magnesium ion coordination in the enzyme active site.
Abstract: The expanded chemical scaffolds of second-generation compounds mediate interactions with the protein backbone that are critical for antagonizing viruses containing the Q148H and G140S mutations.
Introduction: As a start, we analyzed respective side chains in our SIVrcm Q148H/G140S intasome structure.


  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
Abstract: The Y143R/H/C substitutions were the most prevalent, followed by the N155H, and both Q148H/K and G140S/A in the same proportion.
Table: G140S
Discussion: According to our findings, the frequency of the substitution Q148+ >=1 secondary mutation(s) (G140A/C/S, L74I or E138A/K/T) was 12%.



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