Laboratory Molecules of Communication and Adaptation of Microorganisms (MCAM), Muséum National d’Histoire Naturelle, Centre National de la Recherche Scientifique, Paris, France

Sylvie Rebuffat studied chemistry and biochemistry at the University Pierre and Marie Curie in Paris. She then worked on toxins and antifungal peptides from Penicillium and Trichoderma fungi.

Since 1997, S. Rebuffat is professor at the National Museum of Natural History (MNHN). She directed the MNHN-CNRS laboratory Molecules of Communication and Adaptation of Microorganisms over the period 2007-2017. Her major research topic concerns the molecular aspects of the adaptive processes and defence mechanisms developed by microorganisms (bacteria, archaea) in microbiota, through identification of the roles played by the antimicrobial peptides (microcins and bacteriocins) they produce. The molecular mechanisms involved in their biosynthesis (posttranslational modifications introduced by dedicated enzymes that lead to the mature active peptides), their export out of producing bacteria and uptake into susceptible bacteria (recognition by specific receptors at the bacterial membrane), and the identification of their intracellular targets, are studied. The ecological roles of these peptides, their interactions with the gut microbiota and their applications in human or veterinary medicine are currently examined. S. Rebuffat is the author of over 170 publications recorded in the Web of Science and published in international journals or book chapters.

Areas of expertise

Antimicrobial peptides, ribosomally synthesized and posttranslationally modified peptides (RiPPs) and unmodified ribosomally synthesized peptides (URiPs); bacteriocins, microcins, lasso peptide. Biosynthesis of bacteriocins/microcins; Mechanisms of action and of recognition of bacteriocins/microcins (receptors, intracellular targets); Resistance mechanisms of bacteria and archaea to stress (toxic metals; extreme environments); Chemistry, biochemistry of peptides and proteins; three-dimensional structures of peptides.