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



Thierry TOUZE

Group Leader

Research Director


Volunteer Researcher

Muriel MASI





Volunteer Researcher

Rodolphe AUGER


Delphine PATIN



Master Intern


Intern Student

Angélique JONCOUR

Intern Student

Latest publications

For all the publications of the Team click on the button below.

External funding


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


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


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

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