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 HIV mutation literature information.


  Effects of HIV type-1 immune selection on susceptability to integrase inhibitor resistance.
 PMID: 19918099       2009       Antiviral therapy
Introduction: Additionally, the major resistance mutations Q148H/RK and N155S have been shown to reduce replicative capacity.
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.
Result: Of the 38 major and minor integrase inhibitor resistance associated codons, 44, 61, 66, 92, 121, 140, 143, 147, 148, 155, 226 and 263 were the only positions absolutely conserved across all 342 sequences and these included six primary resistance-associated mutations for raltegravir and elvitegravir (T66I


  The use of integrase inhibitors in treatment-experienced patients.
 PMID: 19959414       2009       European journal of medical research
Introduction: A genotypic resistance test could be performed in 38 of these patients of whom 35 selected resistance mutations in the integrase gene following the N155H or the Q148H/R/K path almost always associated with one additional mutation.
Introduction: Overall, by week 96 resistance tests were available for 112 raltegravir treated patients of whom 73% had integrase mutations at one of the three positions (Y143C/H/R, Q148H/K/R N155H) almost always in combination with at least one other mutation.
Introduction: The N155H or the Q148H/R/K alone are associated with high or intermediate levels of resistance that beca


  HIV resistance to raltegravir.
 PMID: 19959417       2009       European journal of medical research
Abstract: HIV resistance to raltegravir is the consequence of mutations located close to the integrase active site, which can be divided into three main evolutionary pathways: the N155H, the Q148R/H/K and the Y143R/C pathways.
Abstract: Resistance is frequently initiated by viruses carrying mutations of the N155H pathway, followed by emergence and further dominance of viral genomes carrying mutations of the Q148R/H/K or of the Y143R/C pathways, which express higher levels of resistance.


  Biochemical analysis of HIV-1 integrase variants resistant to strand transfer inhibitors.
 PMID: 18577511       2008       The Journal of biological chemistry
Abstract: In the case of the Q148R variant, the origin of reduced compound affinity lies in alterations to the active site that reduce the binding of a catalytically essential magnesium ion.
Abstract: The Q148R variant was the most defective enzyme.


  Analysis of natural sequence variation and covariation in human immunodeficiency virus type 1 integrase.
 PMID: 18596095       2008       Journal of virology
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.
 PMID: 18625269       2008       Antiviral research
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.
Abstract: Q148R and F121Y were the two main pathways of resistance to S/GSK-364735.


  Drug resistance profiles for the HIV integrase gene in patients failing raltegravir salvage therapy.
 PMID: 18651855       2008       HIV medicine
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.
Abstract: RESULTS: At the time of VF, RAL-resistance mutations were selected: (i) Q148R in patients 1 and 3; (ii) T66A and E92Q in patient 2.


  Natural variation of HIV-1 group M integrase: implications for a new class of antiretroviral inhibitors.
 PMID: 18687142       2008       Retrovirology
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.
 PMID: 18702518       2008       Biochemistry
Introduction: For raltegravir the two main mutations are N155H or Q148H/R/K with 10- and 25-fold in vivo resistance, respectively.


  Resistance mutations in human immunodeficiency virus type 1 integrase selected with elvitegravir confer reduced susceptibility to a wide range of integrase inhibitors.
 PMID: 18715920       2008       Journal of virology
Abstract: We find the primary resistance-conferring mutations to be Q148R, E92Q, and T66I and demonstrate that they confer a reduction in susceptibility not only to elvitegravir but also to raltegravir (MK-0518) and other integrase inhibitors.



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