literature

HIV mutation literature information.

Consensus HIV-1 FSU-A integrase gene variants electroporated into mice induce polyfunctional antigen-specific CD4+ and CD8+ T cells.

PMID: 23667513 2013 PloS one

Figure: Amino acid sequences of the consensus HIV-1 clade A integrase (IN_a), its inactive variant containing mutation in the active site D64V (IN_in), and inactive variant with mutations conferring resistance to elvitegravir H51Y, E92Q, S147G, E157Q, K160Q (IN_in_e3), all with Met-Gly dipeptide on the N-terminus (A); Schematic representation of the structure of the synthetic genes.

Discussion: For HIV-1 clade A, the main mutations of elvitegravir resistance are H51Y, E92Q, S147G, along with E157Q and a secondary nonpolymorphic mutation, K160Q, highly infrequent in

PMID: 24205814 2013 Journal of chemical information and modeling

Abstract: However, mutants have emerged, such as E92Q/N155H and G140S/Q148H, which confer resistance to raltegravir (RAL), the first IN strand transfer inhibitor (INSTI) approved by the FDA, and to the recently approved elvitegravir (EVG).

Plasma raltegravir exposure influences the antiviral activity and selection of resistance mutations.

PMID: 21457126 2012 AIDS research and human retroviruses

Abstract: Integrase sequences could be obtained for 89 (84%), of whom 30 (33.7%) depicted primary RAL resistance mutations (15 N155H, eight Q148H/R, three Y143R, one E92Q, and three more than one of them).

Three main mutational pathways in HIV-2 lead to high-level raltegravir and elvitegravir resistance: implications for emerging HIV-2 treatment regimens.

PMID: 23028968 2012 PloS one

Table: E92E/Q

Table: E92Q

Figure: Panels B and D show representative dose-response data for WT, Q148R, and G140S+Q148R versus raltegravir and WT, N155H, and E92Q+N155H versus elvitegravir, respectively.

"Prolonged and substantial discordance in prevalence of raltegravir-resistant HIV-1 in plasma versus PBMC samples revealed by 454 ""deep"" sequencing."

PMID: 23049972 2012 PloS one

Introduction: E92Q is also associated with another integrase-inhibitor, elvitegravir.

Introduction: Well-characterized mutations in the HIV-1 int region that confer high levels of resistance to raltegravir include E92Q, Y143R/H/C, Q148H/K/R and N155H.

Method: Primary raltegravir-associated DRMs were defined to be E92Q, Y143R/C/H, Q148H/R/K, and N155H/S (HXB2 int amino acid coordinates), according to the International AIDS Society guidelines.

HIV-1 integrase resistance among antiretroviral treatment naive and experienced patients from Northwestern Poland.

PMID: 23259737 2012 BMC infectious diseases

Abstract: Among 12 (26.1%) raltegravir treated patients treatment failure was observed; major InI drug resistance mutations (G140S, Q148H and N155H, V151I, E92EQ, V151I, G163R) were noted in four of these cases (8.3% of the total InI-treated patients).

Result: Development of drug resistance mutations followed two patterns: major N155H with or without subsequent accessory V151I, E92EQ, V151I, G163R mutants (three cases) and Q148H accompanied by

PMID: 20946407 2011 Clinical microbiology and infection

Abstract: Major mutation sites in the integrase (E92Q, F121Y, G140A/S, Y143C/R, Q148H/R/K and N155H) were not detected, and only a few minor mutation sites (L74M, V151I, E157Q, V165I, I203M, S230N and D232N) were identified in 21 strains (28%).

Resistance associated mutations to dolutegravir (S/GSK1349572) in HIV-infected patients--impact of HIV subtypes and prior raltegravir experience.

PMID: 21439330 2011 Antiviral research

Abstract: T124A was more frequent in INI-naive patients but E92Q and Q148H/R were only seen in raltegravir-experienced individuals.

Abstract: E92Q and Q148H/R were only seen in raltegravir-experienced patients and exclusively infected with subtype B (1.9% vs. 0%, p=0.026, for E92Q and 12.6% vs. 0%, p<0.001, for Q148H/R).

Switching between raltegravir resistance pathways analyzed by deep sequencing.

PMID: 21832937 2011 AIDS (London, England)

Result: We also detected T97A, an accessory mutation for Y143R, and L74M and E92Q, accessory mutations for N155H, from the forward read sets (data not shown).

G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to raltegravir whereas Y143C does not.

PMID: 21854605 2011 Retrovirology

Result: Both enzymes were active in vitro, suggesting that the impairment of the catalytic activity of the T2 IN (E92Q/Y143C) was not directly related to the presence of these mutations (Figure 6A).

Result: By contrast, the resistance level increased when E92Q was introduced into a Y143C resistant background (IC50 = 370 nM), suggesting that the concomitant presence of the two mutations was necessary for this significant increase in resistance.

Result: Like Y143C, E92Q alone did not confer significant resistance to RAL in vitro.

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