Fig. 6: Structure-based escape mutations do not generate viable viruses.
From: Structural insights into tecovirimat antiviral activity and poxvirus resistance
a, Close view of the dimerization interface across the twofold axis showing the designed mutations S292F, S292K and L296Y and the mutation identified in VARV, R291E. The circle indicates the localization of the tecovirimat-binding site. b, Mass-photometry-based dose–response curve showing tecovirimat activity against different mutants, as indicated. Data are mean ± s.d. of three independent experiments (n = 3). c, Viral titres in p.f.u. ml−1 (left panel) and plaque size (right panel) in the presence (+) and absence (−) of 10 µM tecovirimat calculated from plaque assays. Each bar represents the means ± s.d. from two independent experiments (n = 2). The limit of detection (102 p.f.u. ml−1) is indicated with a dashed line.
