literature

HIV mutation literature information.

Therapy-Emergent Drug Resistance to Integrase Strand Transfer Inhibitors in HIV-1 Patients: A Subgroup Meta-Analysis of Clinical Trials.

PMID: 27532886 2016 PloS one

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 indepen

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.

PMID: 27130466 2016 Retrovirology

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.

PMID: 27369381 2016 Nucleic acids research

Abstract: However, these structures give only a partial sense for the limited inhibition of the 3'-processing reaction by INSTIs and how INSTIs can be modified to overcome drug resistance, notably against the G140S-Q148H double mutation.

Abstract: In addition, the G140S-Q148H (SH) mutant integrase, which has

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).

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.

PMID: 27779200 2016 Scientific reports

Method: Besides these three major mutations, the integrase substitutions with a Stanford HIVdb score 10 to at least one INSTI were included, such as H51Y, T66A/I/K, L74M, E92G/Q/V, Q95K, T97A, F121Y, E138A/K, G140S/C/A, Y143G/K/S/A, P145S, Q146P, S147G, V151A/L, S153F/Y, N155S/T,

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

Result: Based on data from these patient-derived isolates, BIC had an improved resistance profile compared to DTG, EVG, and RAL (with mean fold changes of 2.8, 5.8, >106, and >100, respectively; P = 0.04 for BIC versus DTG) and, most notably, against highly INSTI-resistant isolates encoding multiple mutation combinations, such as E92Q/N155H or G140C/S plus Q148R/H/K with or without additional INSTI mutations (P = 0.037 for the 23 isolates with mutations at positions 140 and 148 and P = 0.031 for the 2 isolates with mutations at positions 92 and 155 for BIC versus DTG).

Result: In a side-by-side comparison with DTG, the same variants displayed comparable or, for the G140S/Q148R mutant, even

Drug resistant integrase mutants cause aberrant HIV integrations.

PMID: 27682062 2016 Retrovirology

Conclusion: At least two of the three clinically relevant drug resistant integrase mutants we tested, N155H and G140S/Q148H, which reduce the enzymatic activity of integrase, caused aberrant integrations, even in the absence of any added drug.

Introduction: Two of these mutants, N155H and G140S/Q148H, also had, relative to WT HIV-1, a reduced susceptibility to EVG, and to other INSTIs.

Introduction: We tested the effects of three IN mutations, Y143R, N155H, and the double mutation

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