Result: Collectively, our data revealed three distinct patterns of mutations eliciting resistance to raltegravir in HIV-2: Q148R in one patient, E92Q - T97A in two patients, and N155H - E92A/G/Q in six patients.
Impact of primary elvitegravir resistance-associated mutations in HIV-1 integrase on drug susceptibility and viral replication fitness.
PMID: 23529738
2013
Antimicrobial agents and chemotherapy
Abstra
Abstract: Less commonly observed primary IN mutations also showed a range of reduced EVG susceptibilities: 40- to 94-fold for T66K and Q148K and 5- to 10-fold for T66A, E92G, and Q148H.
Abstract: Primary INSTI resistance-associated mutations (RAMs) at six IN positions have been identified in HIV-1-infected patients failing EVG-containing regimens in clinical studies: T66I/A/K, E92Q/G, T97A, S147G, Q148R/H/K, and N155H.
HIV-2 antiviral potency and selection of drug resistance mutations by the integrase strand transfer inhibitor elvitegravir and NRTIs emtricitabine and tenofovir in vitro.
PMID: 23187937
2013
Journal of acquired immune deficiency syndromes (1999)
Abstract: HIV-2 site-directed mutant (SDM) viruses with E92G and E92Q integrase mutations showed 3.7- and 16-fold reduced susceptibilities to EVG, respectively.
Abstract: In resistance selections, EVG selected E92G/Q and S147N in integrase, FTC selected M184V/I in RT, and TFV selected K65R and Y115F in RT.
Three main mutational pathways in HIV-2 lead to high-level raltegravir and elvitegravir resistance: implications for emerging HIV-2 treatment regimens.
Abstract: Resistance selection experiments using metabolites M1 and M4 led to the development of the previously reported elvitegravir integrase resistance mutations H51Y, T66A, E92G, and S147G, as well as a novel S153F substitution.
G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to raltegravir whereas Y143C does not.
Discussion: Thus, although we did not investigate the effect of E92 mutations on the in vitro resistance of N155H-containing HIV-2 IN, we suggest that the emergence of E92A/G/Q secondary mutations, facilitated by the single nucleotide change required for all substitutions -- E to A, E to G or E to Q transition -- may be involved in the switch from the N155H to the Y143C pathway in the HIV-2 context.
Secondary integrase resistance mutations found in HIV-1 minority quasispecies in integrase therapy-naive patients have little or no effect on susceptibility to integrase inhibitors.
PMID: 20479206
2010
Antimicrobial agents and chemotherapy
Abstract: A novel mutation, E92G, although rarely found in minority quasispecies, showed elvitegravir resistance.
Early emergence of raltegravir resistance mutations in patients receiving HAART salvage regimens.
Abstract: Mutations at positions involved in raltegravir resistance (E92G, G140S, Q148H, and N155H) were detected in 4 of 11 (36.3%) patients as early as 1 month after initiating salvage HAART.
Natural variation of HIV-1 group M integrase: implications for a new class of antiretroviral inhibitors.
HIV mutation literature information.
PMID: 
2014
PloS one
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