Dolutegravir-Selected HIV-1 Containing the N155H and R263K Resistance Substitutions Does Not Acquire Additional Compensatory Mutations under Drug Pressure That Lead to Higher-Level Resistance and Increased Replicative Capacity.
Abstract: To this end, each of the L74M, E92Q, T97A, E157Q, and G163R substitutions were introduced into NL4.3 subtype B HIV-1 vectors harboring N155H and R263K in tandem [termed NL4.3IN(N155H/R263K)].
Abstract: We found that the addition of T97A, E157Q, or G163R somewhat improved the affinity of INN155H/R263K for its target DNA substrate, while the presence of L74M or E92Q had a negative effect on th
Resistance against Integrase Strand Transfer Inhibitors and Relevance to HIV Persistence.
Introduction: We characterized the catalytic activity of INA and its variants containing two major combinations of RALand EVG-resistance mutations: E92Q, V151I, N155H, G163R, L74M (mutant 1), and Q148K, E138K, G140S (mutant 2) .
2014 Update of the drug resistance mutations in HIV-1.
Discussion: Mutations described in the N155H pathway include this major mutation plus either L74M, E92Q, T97A, E92Q plus T97A, Y143H, G163K/R, V151I, or D232N.
Prevalence of primary resistance mutations to integrase inhibitors in treatment-naive and -experienced patients infected with B and non-B HIV-1 variants.
Abstract: According to the geno2pheno algorithm, some of the secondary mutations detected (L74V, E138K, G163RS, and V151I) have been associated with a reduced estimated susceptibility to RAL and only the E138K mutation has been associated with a decreased estimated susceptibility to EGV.
Study of genotypic and phenotypic HIV-1 dynamics of integrase mutations during raltegravir treatment: a refined analysis by ultra-deep 454 pyrosequencing.
PMID: 22238474
2012
The Journal of infectious diseases
Abstract: RESULTS: At baseline, primary resistance mutations were not detected by both population and UDPS genotypic assays; few secondary mutations (T97A-V151I-G163R) were rarely detected and did not show any statistically association either with virologic response at 24-weeks or with the development of resistant variants at failure.
BF integrase genes of HIV-1 circulating in Sao Paulo, Brazil, with a recurrent recombination region.
Abstract: Among 12 (26.1%) raltegravir treated patients treatment failure was observed; major InI drug resistance mutations (G140S, Q148H and N155H, V151I, E92EQ, V151I, G163R) were noted in four of these cases (8.3% of the total InI-treated patients).
Introduction: On the other hand, polymorphic mutations in the central core domain positions have been observed in up to 34% of the published sequences and 56% of the patients with recently acquired infection ; some of these naturally occurring variants have been observed in patients failing raltegravir and elvitegravir (L74M, T97A,
"Prolonged and substantial discordance in prevalence of raltegravir-resistant HIV-1 in plasma versus PBMC samples revealed by 454 ""deep"" sequencing."
Method: Secondary raltegravir-associated DRMs were defined to be E92V, Q95K, T97A, F121Y, E138A/K, G140A/C/S, S147G, V151A/I/L, M154I/L, E157Q, and G163K/R, and linkages examined were T97A and Y143C/R, E138A/K and Q148H/K/R, G140S and Q148H/K/R, and G163K/R and
Subtype diversity associated with the development of HIV-1 resistance to integrase inhibitors.
Abstract: Of note, the remaining patients on RAL regimens for 14 +- 3 months harbored no or only minor integrase mutations/polymorphisms (T66I, T97A, H114P, S119P, A124S, G163R, I203M, R263K).
HIV mutation literature information.
PMID: 
2015
Journal of virology
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