Michel Arthur

TL;DR: Glycopeptide resistance in enterococci results from the production of peptidoglycan precursors with low affinity for these antibiotics, and the mobility of the resistance genes by transposition and conjugation and the ability of the resistant proteins to interfere with synthesis of normal precursor in different hosts indicate that dissemination into other bacterial species should be anticipated.

TL;DR: It is shown that a complex adaptive response thought to endow M. tuberculosis with the capacity to survive several months of combinatorial antibiotic treatment may involve remodeling of the peptidoglycan network by substitution of 4-->3 cross-links generated by the D,D-transpeptidase activity of penicillin-binding proteins by 3-->3Cross- links generated by a transpePTidase of L,D specificity.

TL;DR: This study suggests that a combination of L,D-transpeptidase and β-lactamase inhibitors could effectively target persisting bacilli during the chronic phase of tuberculosis.

TL;DR: It is shown that this mechanism of action can be defeated by a novel type of transpeptidase identified for the first time by reverse genetics in aβ-lactam-resistant mutant of Enterococcus faecium.

TL;DR: The role of antibiotics in selecting or counter-selecting diversification of the structure of peptidoglycan precursors and their mode of polymerization is focused on.