title: O-Acetylated peptidoglycan: controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems.
abstract: The O-acetylation of peptidoglycan is now known to occur in 50 different bacterial species, both Gram positive and Gram negative, including a number of important human pathogens. This modification to the essential cell wall component of bacteria provides both a level of control over endogenous autolysins and protection from the lysozymes of innate immune systems. In this review, we describe the details of the pathways for peptidoglycan O-acetylation that are now beginning to emerge and we explore the possibility that the associated enzymes may present new candidates for antibacterial targets.
authors: Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
authors: Patrick J
authors: PJ
authors: Moynihan
authors: Anthony J
authors: AJ
authors: Clarke
mesh_terms: D000107:Acetylation; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism*; D024881:Drug Resistance, Bacterial; D006090:Gram-Negative Bacteria / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D006801:Humans; D007113:Immunity, Innate / Q000502:physiology*; D008954:Models, Biological; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D010457:Peptidoglycan; D009238:N-Acetylmuramoyl-L-alanine Amidase