File S1 - The Ambiguous Base-Pairing and High Substrate Efficiency of T-705 (Favipiravir) Ribofuranosyl 5′-Triphosphate towards Influenza A Virus Polymerase

Contains: Figure S1. Inhibition of influenza virus RNPs by a nucleoprotein binder. Polyacrylamide gel electrophoresis (6%) result showing the decrease in radiolabeled viral RNA product from the enzymatic reaction in the presence of increasing concentrations of a nucleozin analog used as nucleoprotein inhibitor. Concentrations of inhibitor are as follows: lane 1 (0), lane 2 (0.015), lane 3 (0.046), lane 4 (0.14), lane 5 (0.41), lane 6 (1.2), lane 7 (3.7), lane 8 (11.1), lane 9 (33.3), and lane 10 (100 µM). Figure S2. Determination of ATP substrate efficiency using t14-3 RNA Template. (A) Natural ATP was added to the reaction at increasing concentrations up to 10 µM and the quantitative analysis of AMP incorporation based on the extension of the 9-mer RNA product to the +10 position. (B) The percentage of the extended products from 9-mer was plotted against ATP concentration and the data was fitted to a hyperbolic equation (see Materials and Methods) with a derived Kapp = 0.038 µM for ATP incorporation. The inset shows the same plot on a semi-log scale. Appendix S1. Equation derivation.
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