Post-translational acylation drives folding and activity of the CyaA bacterial toxin.
Corentin C. Leger, Samuel Hoff, Gaia Scilironi, Amiel Abettan, Roshan Shrestha, Jacinthe Frangieh, Vincent Deruelle, Nicolas Carvalho, Dorothée Raoux‐Barbot, Nathalie Duclert‐Savatier, Benjamin Bardiaux, Sébastien Brier, François Bontems, Gérard Pehau‐Arnaudet, Daniel Ladant, , Alexandre Chenal
This study shows that acylation stabilizes the native fold of CyaA and facilitates its membrane orientation, revealing how post-translational modification drives toxin activity.
bioRxiv · Sep 11, 2025 · PreprintBiophysics