Abstract: Viruses containing a Q148R(H) mutation together with a G140S mutation were more resistant to raltegravir than viruses containing a Q148R(H) mutation alone; however, viruses containing G140S and Q148K were more susceptible to raltegravir than viruses containing a Q148K mutation alone.
Effects of HIV type-1 immune selection on susceptability to integrase inhibitor resistance.
Introduction: Major genetic pathways to integrase resistance, initially through N155H and shifting to Q148H/K/R-G140S or directly to Q148H/K/R-G140S, have been reported.
Discussion: In this population-based review of all sites associated with integrase inhibitor resistance in 342 natural isolates of HIV-1 obtained from two geographically distinct cohorts in Switzerland and Australia, we observed that the primary raltegravir and elvitegravir resistance mutations T66I, E92Q, G140S, Y143C/H/R, Q148H/R/K and
Mutations associated with failure of raltegravir treatment affect integrase sensitivity to the inhibitor in vitro.
PMID: 18227187
2008
Antimicrobial agents and chemotherapy
Abstract: All the mutations identified altered the activities of integrase protein: both 3' processing and strand transfer activities were moderately affected in the E92Q mutant; strand transfer was markedly impaired in the N155H mutant; both activities were strongly impaired in the G140S Q148H mutant; and the E157Q mutant was almost completely inactive.
Abstract: At least four genetic profiles (E92Q, G140S Q148H, N155H, and E157Q) can be associated with in vivo treatment failure and resistance to raltegravir.
Abstract: Four different mutation profiles were identified in these nine patients
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.
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,
Discussion: Nearly all INI-resistance mutations known to directly reduce HIV-1 susceptibility were nonpolymorphic including H51Y, T66I, E92Q, F121Y, G140S, Y143C/H/R, Q146P, S147G, Q148H/R/K, S153Y, N155H/S, and R263K.
Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants.
Introduction: Additional mutations have been reported (L74M, E92Q, E138K, G140S/A and G163R).
Preliminary mapping of a putative inhibitor-binding pocket for human immunodeficiency virus type 1 integrase inhibitors.
PMID: 16377678
2006
Antimicrobial agents and chemotherapy
Abstract: Specifically, the single mutations E92K, Q148A, K156A, K156R, G140S, and G149S, as well as the double mutations C65S-K156N and H67D-G140A were evaluated for their effects on enzymatic activity and inhibitor susceptibility.
G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to raltegravir whereas Y143C does not.
Abstract: IN(G140S) was resistant to both L-CA and L-731,988, a diketoacid.
Abstract: HIV containing the G140S mutation showed a delay in replication.
Abstract: In this report, the effects of a glycine to serine mutation at position 140 (G140S) on HIV IN and its effects on IN inhibitor resistance are described.
Abstract: The G140S mutation attenuates IN activity and confers resistance to IN inhibitors, suggesting that diketoacids and L-CA interact with a similar binding site on HIV IN.
Abstract: The mu
Viral entry as the primary target for the anti-HIV activity of chicoric acid and its tetra-acetyl esters.
Abstract: Although inhibition of HIV integrase activity by L-CA and its derivatives was confirmed in an oligonucleotide-driven assay, integrase carrying the G140S mutation was inhibited to the same extent as the wild-type integrase.
Abstract: This conclusion was based on the inhibition of integrase activity in enzymatic assays and the isolation of a resistant HIV strain with a mutation (G140S) in the integrase gene.
HIV mutation literature information.
PMID: 
2009
Journal of virology
Browser Board
Co-occurred Entities
Filtrator
ViMRT