literature

HIV mutation literature information.

Effect of raltegravir resistance mutations in HIV-1 integrase on viral fitness.

PMID: 20634701 2010 Journal of acquired immune deficiency syndromes (1999)

Abstract: Fitness was partially restored by the presence of additional RAL resistance mutations at positions G140S and E92Q or E138K, respectively.

Result: By contrast, the E92Q/N155H mutant was fitter than the E138K/Q148H mutant both in the absence and presence of 5.0 microM RAL (Table 2).

Result: However, the E138K/Q148H mutant was less fit than G140S/Q148H in the absence and presence of drug.

Distinct mutation pathways of non-subtype B HIV-1 during in vitro resistance selection with nonnucleoside reverse transcriptase inhibitors.

PMID: 20805392 2010 Antimicrobial agents and chemotherapy

Abstract: Y181C was the dominant mutation in the resistance selection with etravirine (ETV) in subtype A, and E138K/H221Y were the mutations detected in the breakthrough viruses from subtype C viruses with ETV.

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.

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