Mechanisms of human immunodeficiency virus type 1 concerted integration related to strand transfer inhibition and drug resistance.
PMID: 18591263
2008
Antimicrobial agents and chemotherapy
Abstract: Each mutant exhibited some degree of catalytic impairment relative to the activity of wild type IN, although the N155H mutant displayed near-wild-type IN activities.
Abstract: The S153Y and N155S IN resistance mutants were selected with the diketo acid L-841,411, and the N155H mutant was selected with L-810,812.
Abstract: The N155H mutation confers resistance to L-870,810 and potentiates susceptibility to L-841,411.
Analysis of natural sequence variation and covariation in human immunodeficiency virus type 1 integrase.
Abstract: The critical mutations that determine the resistance pathways to raltegravir and elvitegravir (N155H, Q148K/R/H, and E92Q) were either rare or absent from the 1,165-sequence data set.
Selection of diverse and clinically relevant integrase inhibitor-resistant human immunodeficiency virus type 1 mutants.
Abstract: Q148R/K and N155H, which were found in patients failing raltegravir treatment in Phase IIb studies, were observed during passage with raltegravir with this method.
Drug resistance profiles for the HIV integrase gene in patients failing raltegravir salvage therapy.
Abstract: A gradual accumulation of new mutations was observed in all patients, including G140S, Q148H and N155H in patient 1, L74I in patient 2, and G140S in patient 3.
Abstract: Clonal analysis showed the coexistence, in patient 1, of the two common resistance pathways (mutations Q148R/H and N155H) found in distinct quasi-species.
Natural variation of HIV-1 group M integrase: implications for a new class of antiretroviral inhibitors.
Result: Among the CCD mutations shown to directly reduce raltegravir or elvitegravir susceptibility - H51Y, T66I, E92Q, F121Y, G140S, Y143C/H/R, Q146P, S147G, Q148H/R/K, S153Y, N155H/S, and E157Q - only positions 153 and 157 are polymorphic (prevalence >= 0.5%) with S153A and E157Q each present in 1% of sequences (Figures 1).
Result: The INI-resistance mutation, N155H was present in one subtype B isolate
Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants.
Abstract: The aims of the present study were (1) to investigate and compare the effects of raltegravir and elvi
Discussion: 2.4-fold for the N155H mutant, respectively) might be due to differences in assay conditions and enzyme preparations.
Discussion: IN S153Y and N155H are among the natural polymorphisms analyzed in the present study.
Discussion: Our data extend recent publications for raltegravir showing resistance for the E92Q and the N155H mutants.
Discussion: The second group includes mutations that confer approximately 2-fold less resistance to raltegravir than elvitegravir (T66I, F121Y, Q148K and N155H).
[Resistance to integrase inhibitors].
PMID: 19572425
2008
Enfermedades infecciosas y microbiologia clinica
Abstract: The most frequently observed mutations in failure with elvitegravir are E92Q, E138K, Q148R/K/H and N155H, and less frequently S147G and T66A/I/K.
Abstract: Virologic failure with raltegravir is associated with selection of primary mutations such as N155H (40%) and distinct changes in position Q148 (28%).
Natural polymorphism of the HIV-1 integrase gene and mutations associated with integrase inhibitor resistance.
Abstract: Of the 42 aa substitutions currently associated with INI resistance, 21 occurred as natural polymorphisms: V72I, L74I, T97A, T112I, A128T, E138K, Q148H, V151I, S153Y/A, M154I, N155H, K156N, E157Q, G163R, V165I, V201I, I203M, T206S, S230N and R263K.
HIV mutation literature information.
PMID: 
2008
Antimicrobial agents and chemotherapy
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