Using a dual-luciferase assay, they concluded that the compound functions by enhancing the frameshifting efficiency of the HIV-1 ribosomal frameshift signal, resulting in a decrease in the Gag/Gag-Pol protein ratio and thereby preventing the proper maturation of the viral particle and ultimately inhibiting infection. Moving forward, structural studies of the interactions between the lead compound and the downstream secondary RNA structure of the HIV-1 ribosomal frameshift signal will be vital to understanding the reason for high affinity and the method of action.
Through a dual-luciferase assay, they found that the compound boosts the efficiency of frameshifting in the HIV-1 ribosomal frameshift signal, causing a drop in the Gag/Gag-Pol protein ratio and thus preventing the correct formation of the viral particle and ultimately stopping infection. Further research on the interactions between the lead compound and the downstream RNA structure of the HIV-1 ribosomal frameshift signal will be essential to understand why it has high affinity and how it works.