Stéphane Mesnage

The paper characterizes ORF11, a tail-spike lysin from E. faecium Minhovirus, revealing its dual peptidoglycan hydrolysis activity through structural and biochemical analysis.

This study characterizes LdtRj8, an LDT enzyme from Rhizobium johnstonii, showing pH-dependent activity and broad amino acid substrate specificity, which may explain muropeptide isomerism and bacterial adaptation to acidic environments.

This study identifies 33 distinct domain architectures of prophage endolysins from enterococci, including a novel cell wall-binding domain, to expand the diversity of potential enzybiotics against multidrug-resistant infections.

This paper identifies AtlE, an N-acetylmuramidase essential for virulence in E. faecalis, showing its role in cell wall remodelling and immune evasion via the release of EPA-containing fragments.

This study determines the structure of the Enterococcal Polysaccharide Antigen (EPA) from E. faecalis and explores its role in immune evasion and phage susceptibility.

This study develops an in vitro assay to investigate how EPA decorations on E. faecalis affect phagocytosis, showing that decoration deletion increases phagocytosis and that lipoproteins are not involved.

The paper identifies 1-3 peptidoglycan cross-links in Gluconobacter oxydans using modified PGFinder software and discovers an L,D-transpeptidase with a YkuD-related domain responsible for these cross-links.