Bacterial Cell Envelopes
and Antibiotics
The team investigates the metabolism of peptidoglycan, which is the main constituent of the bacterial cell wall. This exoskeleton is essential for cell integrity, division and morphogenesis. It is the target of a large number of antibacterial agents, including antibiotics, with a wide variety of structures and mechanisms of action. Our project aims to better understand underexplored membrane steps in peptidoglycan biosynthesis and to study/design new molecules capable of interfering with these steps for therapeutic purposes.
Structure of peptidoglycan from Escherichia Coli
Peptidoglycan is composed of long glycan chains, which are cross-linked via short peptide stems. Its disaccharide-peptide subunit is polymerized on the outer side of the membrane by the conjugated action of glycosyltransferases and transpeptidases enzymes. The subunit is first assembled on the undecaprenyl phosphate (C55-P) carrier lipid from two nucleotide precursors, UDP-GlcNAc and UDP-MurNAc-peptide. The membrane intermediate thus formed, lipid II, is translocated across the membrane to allow the transfer of the subunit to the peptidoglycan polymer in elongation. The lipid carrier is released as undecaprenyl pyrophosphate (C55-PP), which is recycled. Finally, the peptidoglycan undergoes a series of species-specific maturation and decoration reactions that may confer resistance to antimicrobial agents or allow bacteria to escape recognition by the host immune system.
Biosynthesis of peptidoglycan
Topics
team
Group Leader Professor
Lecturer
Volunteer Researcher
Engineer
Engineer
PhD student
Master Student
Bachelor Student
Master Student
team
Thierry TOUZE
Group Leader
Professor
Hélène BARRETEAU
Assistant Professor
Didier BLANOT
Volunteer Researcher
Rodolphe AUGER
Engineer
Delphine PATIN
Engineer
Victor FOLCHER
Ph D student
Lisa BAL
Ph D student
Latest publications
For all the publications of the Team click on the button below.
External funding
Collaborations
Université Paris-Saclay
Van Tilbeurgh H., I2BC, biologie structurale des bactériocines
Tissières P. et Augusto L., I2BC, marquage et analyse de l’enveloppe
Serror P., INRAE-MICALIS, Jouy-en-Josas, étude de la bactériocine ciblant E. faecalis
Chastanet A., INRAE-MICALIS, Jouy-en-Josas, étude des relations entre C55-PP phosphatases et machineries de synthèse du peptidoglycane
Chapot-Chartier M.-P., INRAE-MICALIS, Jouy-en-Josas, synthèse des polysaccharides de L. lactis
National
Arthur M., INSERM, Centre de Recherche des Cordeliers, Paris, étude des relations entre C55-PP phosphatases et PBPs
Gomperts-Boneca I., Institut Pasteur, Paris, étude du recyclage du C55-P chez Helicobacter pylori et E. coli
Gravier-Pelletier C., University Paris-Descartes, Paris, recherche d’inhibiteurs de MraY
Duché D. et Louot L., LISM, CNRS, Marseille, import des colicines
International
Caffrey M., Trinity College Dublin, Ireland, cristallogenèse des C55-PP phosphatases
Gobec S., University of Ljubljana, Slovenia, criblage virtuel d’inhibiteurs
Kerff F. and Terrak M., University of Liège, Belgium, cristallogenèse des C55-PP phosphatases
Pohl P., University of Linz, Austria, mise en evidence d’une activité C55-P flippase