literature

HIV mutation literature information.

Reduced HIV-1 integrase flexibility as a mechanism for raltegravir resistance.

PMID: 23891838 2013 Journal of structural biology

Abstract: Obtaining crystallographic structure information on the Q148H/R, G140S/A primary and secondary mutations has been elusive.

Dolutegravir interactions with HIV-1 integrase-DNA: structural rationale for drug resistance and dissociation kinetics.

PMID: 24146996 2013 PloS one

Abstract: Signature HIV-1 integrase mutations associated with clinical raltegravir resistance involve 1 of 3 primary genetic pathways, Y143C/R, Q148H/K/R and N155H, the latter 2 of which confer cross-resistance to elvitegravir.

Introduction: In our efforts to structurally rationalize DTG's distinct resistance and dissociation kinetics profiles, we constructed wild-type, Q148R, Q148K, Q148H/G140S and N155H HIV-1 IN models in complex with U5 LTR DNA using carefully selected structural data from wild-type and mutant PFV intasomes as well as Tn5 transposase to model key missing active-site el

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).

Study of genotypic and phenotypic HIV-1 dynamics of integrase mutations during raltegravir treatment: a refined analysis by ultra-deep 454 pyrosequencing.

PMID: 22238474 2012 The Journal of infectious diseases

Abstract: At UDPS, not all resistant variants appearing early during treatment evolved as major populations during failure; only specific resistance pathways (Y143R-Q148H/R-N155H) associated with an increased rate of fitness and phenotypic resistance were selected.

Substitutions at amino acid positions 143, 148, and 155 of HIV-1 integrase define distinct genetic barriers to raltegravir resistance in vivo.

PMID: 22553340 2012 Journal of virology

Abstract: Furthermore, shifts from the N155H pathway to either the Q148R or H pathway or the Y143R pathway were dependent on the amino acid substitution at position 148 and the secondary mutations in Y143R- or Q148R- or H-containing variants and correlated with reductions in RAL susceptibility and restorations in RC.

Abstract: Patient viruses containing Y143R, Q148R, or Q148H mutations consistently exhibited larger reductions in RAL susceptibility than patient viruses containing N155H mutations.

The activity of the integrase inhibitor dolutegravir against HIV-1 variants isolated from raltegravir-treated adults.

PMID: 22878423 2012 Journal of acquired immune deficiency syndromes (1999)

Abstract: The median fold change to dolutegravir for isolates containing changes at G140S + Q148H, G140S + Q148R, T97A + Y143R, and N155H (thus including raltegravir signature resistance codons) were 3.75, 13.3, 1.05, and 1.37, respectively.

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

Abstract: Collectively, our data define three major mutational pathways to high-level raltegravir and elvitegravir resistance: i) E92Q+Y143C or T97A+Y143C, ii) G140S+Q148R, and iii) E92Q+N155H.

Result: Collectively, these data show that raltegravir-resistant mutants of HIV-2 are cross-resistant to elvitegravir and that substitutions T97A+143C, Q148K/R, G140S+Q148R and E92Q+N155H confer high-level elvitegravir resistance in HIV-2.

Result: In contrast, replacements

"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: E138K and G140S are secondary mutations that develop following the detection of Q148K/R, restoring viral infectivity and replication kinetics.

Introduction: Post-raltegravir-therapy evolution of raltegravir-associated DRMs in plasma samples is relatively well-characterized, with reports showing Q148H/K/R+G140S and N155H emerged before Y143R/H/C.

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.

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

PMID: 23259737 2012 BMC infectious diseases

Introduction: Virologic failure has been associated with major, signature mutations within the catalytic domain of the enzyme, and include Y143R/C, N155H Q148K/R/H integrase sequence variants associated with significant susceptibility reduction both to RAL and elvitegravir (EVG) .

Genetic variation of the HIV-1 integrase region in newly diagnosed anti-retroviral drug-naive patients with HIV/AIDS in Korea.

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%).

Browser Board

Co-occurred Entities

Filtrator