literature

HIV mutation literature information.

The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation.

PMID: 19129221 2009 Nucleic acids research

Method: In parallel, the E92Q, G140S, Q148H, N155H and Figure: WT+RAL (open square), WT (filled square), E92Q (gray diamond), G140S (filled diamond), Q148H (filled triangle), N155H (gray circle), G140S/Q148H (filled circle), G140S/Q148H+Ral (open circle), WT + AZT (straight line).

Discussion: These mutations are E92Q, N155H and the G140S/Q148H double mutation, which seems to appear preferentially.

Characterization and structural analysis of HIV-1 integrase conservation.

PMID: 19290031 2009 AIDS reviews

Abstract: All primary signature mutations emerging in patients failing raltegravir (Y143R, Q148H/K/R, N155H) or elvitegravir (T66I, E92Q, S147G, Q148H/K/R, N155H), as well as secondary mutations (H51Y, T66A/K, E138K, G140S/A/C, Y143C/H, K160N, R166S, E170A, S230R, D232N, R263K) were complete

Genetic barriers for integrase inhibitor drug resistance in HIV type-1 B and CRF02_AG subtypes.

PMID: 19320246 2009 Antiviral therapy

Abstract: CONCLUSIONS: The major IN mutations E92Q, Q148K/R/H, N155H and E157Q (implicated in the resistance of IN inhibitors RAL and EVG) are highly conserved between subtypes B and CRF02_AG and display a similar genetic barrier.

Analysis of pol integrase sequences in diverse HIV type 1 strains using a prototype genotyping assay.

PMID: 19327053 2009 AIDS research and human retroviruses

Abstract: Two samples had E92Q (both subtype B) and eight had E157Q (2A, 1C, 1D, 1F, 3 CRF02_AG).

Loss of raltegravir susceptibility by human immunodeficiency virus type 1 is conferred via multiple nonoverlapping genetic pathways.

PMID: 19759152 2009 Journal of virology

Abstract: Analysis of site-directed mutants indicated that E92Q in combination with N155H resulted in a higher level of resistance to raltegravir than N155H alone.

Effects of HIV type-1 immune selection on susceptability to integrase inhibitor resistance.

PMID: 19918099 2009 Antiviral therapy

Introduction: Elvitegravir, which remains in the final stages of clinical development, is additionally associated with T66I and E92Q in primary resistance.

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, E92Q, G140S, Y143C/H/R Q148H/R/K and N155S/H).

Discussion: In this population-based review of all sites associated with integrase inhibitor

Broad antiretroviral activity and resistance profile of the novel human immunodeficiency virus integrase inhibitor elvitegravir (JTK-303/GS-9137).

PMID: 17977962 2008 Journal of virology

Abstract: Among the observed IN mutations, T66I and E92Q substitutions mainly contributed to EVG resistance.

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

Mutations in human immunodeficiency virus type 1 integrase confer resistance to the naphthyridine L-870,810 and cross-resistance to the clinical trial drug GS-9137.

PMID: 18378713 2008 Antimicrobial agents and chemotherapy

Abstract: In conclusion, the accumulation of L74M, E92Q, and S230N mutations in the integrase causes resistance to the naphthyridine L-870,810 and cross-resistance to GS-9137.

Abstract: The L74M and E92Q mutations have both been associated in the past with resistance against the diketo acid (DKA) analogues L-708,906 and S-1360 and the clinical trial drugs MK-0518 and GS-9137.

Abstract: The mutations L74M, E92Q, and S230N were successively selected in the integrase.

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.

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