literature

HIV mutation literature information.

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.

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

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.

Drug resistance profiles for the HIV integrase gene in patients failing raltegravir salvage therapy.

PMID: 18651855 2008 HIV medicine

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.

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.

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 to integrase inhibitors].

PMID: 19572425 2008 Enfermedades infecciosas y microbiologia clinica

Abstract: The most frequently observed mutations in failure with elvitegravir are E92Q, E138K, Q148R/K/H and N155H, and less frequently S147G and T66A/I/K.

Natural polymorphism of the HIV-1 integrase gene and mutations associated with integrase inhibitor resistance.

PMID: 17668566 2007 Antiviral therapy

Abstract: Of the 42 aa substitutions currently associated with INI resistance, 21 occurred as natural polymorphisms: V72I, L74I, T97A, T112I, A128T, E138K, Q148H, V151I, S153Y/A, M154I, N155H, K156N, E157Q, G163R, V165I, V201I, I203M, T206S, S230N and R263K.

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