Method: Patients with more than one darunavir resistance-associated mutation or with known major integrase resistance-associated mutations (N155H, Q148H/R/K, Y143C/R, and G140S) were excluded from the study.
HIV-2 integrase polymorphisms and longitudinal genotypic analysis of HIV-2 infected patients failing a raltegravir-containing regimen.
Result: Collectively, our data revealed three distinct patterns of mutations eliciting resistance to raltegravir in HIV-2: Q148R in one patient, E92Q - T97A in two patients, and N155H - E92A/G/Q in six patients.
Comparative replication capacity of raltegravir-resistant strains and antiviral activity of the new-generation integrase inhibitor dolutegravir in human primary macrophages and lymphocytes.
PMID: 24860155
2014
The Journal of antimicrobial chemotherapy
Abstract: In C8166 (the only cell model in which replication capacity was sufficient to perform the test) dolutegravir showed full efficacy against mutations N155H + Y143C (dolutegravir fold-change resistance: 0.6) and a slightly lower activity against G140S+Q148H (dolutegravir fold-change resistance: 2.1).
Abstract: In MDMs and PBMCs, a dramatic decrease in viral replication was observed for the double mutants N155H + Y143C and G140S +
Abstract: In all cellular models analysed, dolutegravir showed full efficacy against N155H and Y143C mutants (dolutegravir fold-change resistance ranging from 0.1 to 1.4; raltegravir fold-change resistance ranging from 0.1 to 10.3).
Effect of HIV-1 integrase resistance mutations when introduced into SIVmac239 on susceptibility to integrase strand transfer inhibitors.
Abstract: In contrast, Y143R, Q148R, and N155H all yielded low levels of resistance to RAL.
Abstract: Using TZM-bl cells, we demonstrated that the Q148R and N155H mutational pathways conferred resistance to EVG (36- and 62-fold, respectively), whereas R263K also displayed moderate resistance to EVG (12-fold).
In vitro analysis of the susceptibility of HIV-1 subtype A and CRF01_AE integrases to raltegravir.
PMID: 24935032
2014
International journal of antimicrobial agents
Abstract: Enzymatic activities of subtype A and CRF01_AE INs were analysed with regard to typical 3'-end processing (3'-P) and strand transfer (ST) activities both in the presence and absence of RAL and were compared with subtype B IN as well as with the corresponding INs harbouring the N155H resistance mutation.
Abstract: Subtype A and CRF01_AE INs encoded by these consensus sequences as well as the corresponding enzymes harbouring the N155H resistance mutation were expressed and purified.
Abstract: The three INs harbouring the N155H mutation presented in vitro low but similar resistance levels to RAL.
2014 Update of the drug resistance mutations in HIV-1.
Discussion: Cross-resistance studies with raltegravir- and elvitegravir-resistant viruses indicate that Q148H and G140S in combination with mutations L74I/M, E92Q, T97A, E138A/K, G140A, or N155H are associated with 5-fold to 20-fold reduced dolutegravir susceptibility and reduced virologic suppression in patients.
Discussion: Mutations described in the N155H pathway include this major mutation plus either L74M, E92Q, T97A, E92Q plus T97A, Y143H, PMID: 25350960
2014
HIV clinical trials
Abstract: Emergent substitutions were E92Q, N155H, or Q148R (n = 2 each) and T66I or T97A (n = 1 each) in IN and M184V/I (n = 7) and K65R (n = 1) in RT.
Molecular dynamics simulation studies of the wild type and E92Q/N155H mutant of Elvitegravir-resistance HIV-1 integrase.
PMID: 25373632
2014
Interdisciplinary sciences, computational life sciences
Abstract: Although Elvitegravir (EVG) is a newly developed antiretrovirals drug to treat the acquired immunodeficiency syndrome (AIDS), drug resistance has already been found in clinic, such as E92Q/N155H and Q148H/G140S.
Abstract: As full length crystal structure for HIV-1 integrase is still unsolved, we herein use the crystal structure of the full length prototype foamy virus (PFV) in complex with virus DNA and inhibitor Elvitegravir as a template to construct the wild type and E92Q/N155H mutant system of HIV-1 integrase.
Abstract: Molecular dynamic simulations was used to revel the binding mode and the drug resistance of the EVG
HIV-1 group O integrase displays lower susceptibility to raltegravir and has a different mutational pathway for resistance than HIV-1 group M.
PMID: 25397483
2014
Journal of the International AIDS Society
Abstract: None of the HIV-O viruses selected either N155H or Y143C.
New dolutegravir resistance pattern identified in a patient failing antiretroviral therapy.
PMID: 25397494
2014
Journal of the International AIDS Society
Abstract: Here, we present a case of virological failure in a DTG treated patient based on N155H mutation background.
Abstract: However, there is only rare data available about the impact of N155H in the context of secondary site integrase mutations.
Abstract: In June 2013, after S119R, N155H and E157Q mutations in viral integrase were detected, the patient received DTG, and RAL was stopped.
Abstract: Since N155H alone is described not to contribute sufficient resistance to DTG, there seems to be a need to re-check viruses with N155H plus minor mutations (like T97A, S119R,
HIV mutation literature information.
PMID: 
2014
PloS one
Browser Board
Co-occurred Entities
Filtrator
ViMRT