Result: Among the CCD mutations shown to directly reduce raltegravir or elvitegravir susceptibility - H51Y, T66I, E92Q, F121Y, G140S, Y143C/H/R, Q146P, S147G, Q148H/R/K, S153Y, N155H/S, and E157Q - only positions 153 and 157 are polymorphic (prevalence >= 0.5%) with S153A and E157Q each present in 1% of sequences (Figures 1).
Result: The INI-resistance mutations Q148H (subtype G) and
Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants.
Figure: C Defective 3'-P of the Q148K mutant shown as densitometry analysis of the gel presented in panel B (lanes 1, 4 and 7).
Figure: Gel image of typical 3'-P and ST reactions using three different concentrations of Q148K, and showing defective ST and 3'-P activities of the Q148K mutant HIV-1 integrase.
Discussion: The second group includes mutations that confer approximately 2-fold less resistance to raltegravir than elvitegravir (T66I, F121Y, Q148K and N155H).
Discussion: The three most resistant enzymes (Q148K, T66I and S153Y) were also most defective in ST activity.
[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.
HIV mutation literature information.
PMID: 
2008
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