Author

Corentin C. Leger

Centre National de la Recherche ScientifiqueORCID 0000-0002-8293-1356Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 1 Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

Alexandre ChenaliD· 2 shared Daniel LadantiD· 2 shared Dorothée Raoux‐Barbot· 2 shared Gaia Scilironi· 2 shared Jacinthe FrangiehiD· 2 shared Nicolas CarvalhoiD· 2 shared Amiel Abettan· 1 shared Benjamin BardiauxiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

Alexandre ChenalORCID

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2 papers

Recent·Most cited

Covalently linked peptides and membrane potential enable CyaA segment translocation

Gaia Scilironi, Nicolas Carvalho, Jacinthe Frangieh, Corentin C. Leger, Dorothée Raoux‐Barbot, J. Iñaki Guijarro, Daniel Ladant, Sophie Cribier, Nicolás Rodríguez, Alexandre Chenal

This study investigates the translocation mechanisms of two CyaA-derived peptides, showing that P454 translocates independently of membrane potential while P233 requires a negative potential, and their covalent linkage enables translocation without potential.

Advanced Science · Aug 21, 2026Peer-reviewedBiophysics

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