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 HIV mutation literature information.


  Dynamic escape of pre-existing raltegravir-resistant HIV-1 from raltegravir selection pressure.
 PMID: 20883724       2010       Antiviral research
Abstract: Double 148R+N155H mutants were also detected in 1.7% of viruses at virological failure in association with E138K and/or G163R.


  Update of the drug resistance mutations in HIV-1: December 2010.
 PMID: 21245516       2010       Topics in HIV medicine
Abstract: This update includes 9 new mutations- E138G and E138K for etravirine (Haddad M et al, CROI, 2010; Abstract 574, and Vingerhoets J et al, Antivir Ther, 2010;15 [Suppl 2]:A125); E92Q for raltegravir (Geretti AM et al, Antivir Ther, 2010;15 [Suppl 2]:A62; Cooper et al, N Engl J Med, 2008;359:355-365; and Malet I et al, Antimicrob Agents Chemother, 2008;52:1351-1358); and M36L, M36V, H69R, L89I, L89M, and L89V for tipranavir/ritonavir.


  Secondary mutations in viruses resistant to HIV-1 integrase inhibitors that restore viral infectivity and replication kinetics.
 PMID: 19027039       2009       Antiviral research
Abstract: In contrast, Q148K/G140S and Q148R/E138K had nearly equivalent or slightly reduced fold resistance to the INI compared with their respective Q148 primary mutants, and had increases in infectivity and replication kinetics.
Abstract: Relative to Q148K alone, Q148K/E138K had 2- and >6-fold increases in resistance to S-1360 and S/GSK-364735, respectively, and the double mutant had slightly better infectivity and replication kinetics.
Abstract: Secondary amino acid substitutions E138K or G140S were observed when passage with INI was continued.


  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


  Compilation and prevalence of mutations associated with resistance to non-nucleoside reverse transcriptase inhibitors.
 PMID: 19320243       2009       Antiviral therapy
Abstract: These included V90I, A98G, L100I, K1O1E/P/Q, K103H/N/S/T, V106A/I/M, V108I, E138G/K/Q, V179D/E/F/G/I, Y181C/I/V, Y188C/H/L, V189I, G190A/C/E/Q/S, H221Y, P225H, F227C/L, M230I/L, P236L, K238N/T and Y318F


  Natural variation of HIV-1 group M integrase: implications for a new class of antiretroviral inhibitors.
 PMID: 18687142       2008       Retrovirology
Result: Among mutations selected by raltegravir or elvitegravir that have not been shown to directly reduce susceptibility, L74R, Q95K, E138A/K, and H183P were conserved, whereas V54I, L68V, L74M, T97A, V151I, G163R, and I203M were present in approximately 1% to 2% of isolates from untreated persons (Figure 1).
Discussion: Most accessory INI-resistance mutations including L74R, Q95K, E138A/K, H183P,  PMID: 18702518       2008       Biochemistry
Introduction: Additional mutations have been reported (L74M, E92Q, E138K, G140S/A and G163R).
Introduction: Other mutations reported for elvitegravir are H51Y, T66I, Q95K, E138K, Q146P, S147G and E157Q.


  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: In addition, mutations that do not confer reduced susceptibility when present alone (H114Y, L74M, R20K, A128T, E138K, and S230R) are also discussed in relation to their position in the catalytic core domain and their proximity to known structural features of integrase.


  Binding modes of two novel non-nucleoside reverse transcriptase inhibitors, YM-215389 and YM-228855, to HIV type-1 reverse transcriptase.
 PMID: 19024630       2008       Antiviral chemistry & chemotherapy
Abstract: A single amino acid substitution confers only moderate resistance to YM-215389; indeed, four amino acid substitutions (V106L, V108I, E138K and L214F) were necessary for high-level resistance.


  [Resistance to integrase inhibitors].
 PMID: 19572425       2008       Enfermedades infecciosas y microbiologia clinica
Abstract: The most common resistance pattern seems to be E138K + E147G + Q148R.
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.



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