HIV-1 integrase sequence variability in antiretroviral naive patients and in triple-class experienced patients subsequently treated with raltegravir.
PMID: 20961278
2010
AIDS research and human retroviruses
Abstract: Four ARV-naive (5.3%) and two ARV-treated patients (2.7%) had one of the following minor INI-resistance mutations: L74M, E157Q, G163R, and R263K but there was no association between baseline raltegravir genotype and subsequent response to raltegravir treatment.
Dynamic escape of pre-existing raltegravir-resistant HIV-1 from raltegravir selection pressure.
Abstract: Double 148R+N155H mutants were also detected in 1.7% of viruses at virological failure in association with E138K and/or G163R.
Specific HIV-1 integrase polymorphisms change their prevalence in untreated versus antiretroviral-treated HIV-1-infected patients, all naive to integrase inhibitors.
PMID: 20817922
2010
The Journal of antimicrobial chemotherapy
Abstract: Similarly, V165I and G163R mutations were associated with the RT resistance mutations F227L and M230L, respectively, and the T206S polymorphism was associated with the RT resistance mutation L210W.
Effect of raltegravir resistance mutations in HIV-1 integrase on viral fitness.
PMID: 20634701
2010
Journal of acquired immune deficiency syndromes (1999)
Result: Introduction of E92Q or G163R into an N155H backbone resulted in a virus with greater fitness than N155H mutant both in the absence and presence of RAL.
Result: The addition of secondary mutations L74M or E92Q to N155H resulted in 28- and 55-fold resistance, respectively, but addition of G163R did not result in any substantial change in raltegravir resistance.
Result: The relative fitness difference for N155H/G163R versus N155H was 3.4-fold in absence of drug, and 2.1-fold in the presence of RAL.
Result: To determine how the secondary RAL resistance mutations PMID: 20436677
2010
PloS one
Method: We followed-up the 50 mutations of resistance present at 32 positions: associated with in vitro or in vivo resistance to HIV-1 integrase inhibitors: H51Y, T66I/A/K, V72I, L74I/A/M, E92Q, T97A, T112I, F121Y, T125K, A128T, E138 K/A/D, G140R/C/H, Y143C/H/R, Q146K/P, S147G, Q148K/R/H, V151I, PMID: 19770695
2010
AIDS (London, England)
Abstract: The first had the mutations G140S+Q148H+S230N, the second had Y143R+G163R and the third had no evidence of genotypic resistance in integrase.
Effects of HIV type-1 immune selection on susceptability to integrase inhibitor resistance.
Result: There were 18 codons at which at least one sequence contained a (non-primary) drug resistance-associated mutation and in nine of these codons, the prevalence of the resistance mutation exceeded 5% in either the SHCS or WAHCS (M50I prevalence 18.0% and 14.8%, V72I 52.2% and 58.8%, T112I 5.6% and 6.3%, S119G 6.2% and 7.3%, K156N 5.7% and 8.0%, G163A/E/Q/T/R 5.1% and 4.4%, V201I 48.1% and 46.8%, T206S 15.6% and 9.3%, and S230N 9.4% and 6.2% for the SHCS and the WAHCS, respectively; Figure 2A).
Defining the DNA substrate binding sites on HIV-1 integrase.
Result: As previously reported, the G163R Q164V V165L chimera in the 3CSF185H background cleaved both HIV-1 U5 and ASV U3 LTR end substrates (Figure 2).
Result: Twelve of the fifteen amino acid exchanges that affect LTR recognition in the processing reaction were combined into a single construct (V72W S153R K160D I161R G163R Q164V V165L H171K L172Q D229I S230E PMID: 19203393
2009
Retrovirology
Introduction: T97A, V151I, G163R, I203M and S230N) remains unknown.
Characterization and structural analysis of HIV-1 integrase conservation.
Abstract: Differently, other mutations (L74M, T97A, S119G/R, V151I, K156N, E157Q, G163K/R, V165I, I203M, T206S, S230N) occurred as natural polymorphisms with a different prevalence according to different HIV-1 subtype/circulating recombinant form/group.
HIV mutation literature information.
PMID: 
2010
AIDS research and human retroviruses
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