Discussion: Secondary integrase mutations(G140S/G and T97T/A) usually appeared together with Q148H/R and Y143Y/H.
Transmitted drug resistance of HIV-1 strains among individuals attending voluntary counselling and testing in Taiwan.
PMID: 26404079
2016
The Journal of antimicrobial chemotherapy
Abstract: Among the seven major integrase mutations (T66I, E92Q, G140S, Y143C/H/R, S147G, Q148H/K/R and N155H), only one strain harbouring the Q148R mutation was detected.
Q148N, a Novel Integrase Inhibitor Resistance Mutation Associated with Low-Level Reduction in Elvitegravir Susceptibility.
PMID: 27009474
2016
AIDS research and human retroviruses
Abstract: Infectious molecular HIV-1 clones containing Q148N alone and in combination with G140S demonstrated ~2.4-4.5 reduced elvitegravir susceptibility depending on the virus's genetic context but retained susceptibility to raltegravir and dolutegravir.
Introduction: Although the patient's genotypic resistance test was reported as being associated with intermediate resistance to raltegravir and elvitegravir based on the presence of G140S, no change to therapy was made because of the patient's virological and immunological response to therapy.
Introduction: It also contained a recombinant infectious molecular clone from the patient's August 2014 sample and clones in which G140S alone and G140S and Q148N were independently mutated back to the wild type residues at these pos
The design of 8-hydroxyquinoline tetracyclic lactams as HIV-1 integrase strand transfer inhibitors.
PMID: 27092410
2016
European journal of medicinal chemistry
Abstract: This manuscript describes a number of 8-hydroxyquinoline tetracyclic lactams with exceptional antiviral activity against HIV-1 and little loss of potency against the IN signature resistance mutations Q148K and G140S/Q148H.
Effect on HIV-1 viral replication capacity of DTG-resistance mutations in NRTI/NNRTI resistant viruses.
Introduction: The absence of compensatory secondary mutations for R263K is also consistent with the observation that many major RAL- and EVG-resistance substitutions such as G140S, Q148R, E92Q, N155H and Y143R are incompatible with the simultaneous presence of R263K in terms of both integrase strand-transfer activity and viral replication capacity.
Selectivity for strand-transfer over 3'-processing and susceptibility to clinical resistance of HIV-1 integrase inhibitors are driven by key enzyme-DNA interactions in the active site.
Introduction: Using recombinant enzymes and oligonucleotides mimicking the ends of the retroviral DNA, IN mutants have been extensively characterized and RAL resistance can be recapitulated with three primary mutants: Y143R, N155H and G140S-Q148H (SH).
Figure: Differential 3'-processing of modified DNA substrates by the wild-type IN (WT) and the drug-resistant IN mutant G140S-Q148H (SH), and inhibition of 3-processing by raltegravir (RAL) and dolutegravir (DTG).
Figure: Modeling of the WT and G140S-Q148H (SH) IN active sites in complexes with the modified substra
Development of a phenotypic susceptibility assay for HIV-1 integrase inhibitors.
PMID: 27737783
2016
Journal of virological methods
Abstract: Solely a Q148H+G140S variant presented reduced susceptibility to dolutegravir.
Prevalence of Integrase Strand Transfer Inhibitors (INSTI) Resistance Mutations in Taiwan.
Result: Among the INSTI-experienced patients, only one (1.6%) had Q148H/R/K along with two or three of G140A/C/S, L74I and E138A/K/T mutations and were predicted to have high-level resistance to dolutegravir.
Result: The prevalence of T97A, G140CAS, E157Q, and V151I was all significantly higher in specimens from raltegravir-experienced patients than those from INSTI-naive patients.
Result: Twelve sequences (19.1%) had Q148H/R/K with one G140A/C/S, L74I,
Antiviral Activity of Bictegravir (GS-9883), a Novel Potent HIV-1 Integrase Strand Transfer Inhibitor with an Improved Resistance Profile.
PMID: 27645238
2016
Antimicrobial agents and chemotherapy
Figure: Primary INSTI resistance mutations are T66I/A/K, E92Q/G, T97A, Y143C/H/R, S147G, Q148H/K/R, and N155H, and other INSTI resistance mutations are H51Y, L68I/V, V72A/N/T, L74M, Q95K/R, F121C/Y, A128T, E138A/K, G140A/C/S, P145S, PMID: 27682062
2016
Retrovirology
Abstract: More importantly, we show that at least two of the three clinically relevant drug resistant integrase mutants we tested, N155H and G140S/Q148H, which reduce the enzymatic activity of
Result: The G140S mutation is adjacent to Q148H.
Result: We tested three IN mutants, all of which reduced the susceptibility of the virus (and IN) to RAL, and caused a reduction in the relative infectivity of the single-round HIV vector used in our assay system (Y143R, residual titer is 40-45 % of WT; N155H, ~40 % of WT, and G140S/Q148H, 30-35 % of WT).
HIV mutation literature information.
PMID: 
2016
PloS one
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