O-Acetylation of peptidoglycan is required for proper cell separation and S-layer anchoring in Bacillus anthracis.
O-Acetylation of the MurNAc moiety of peptidoglycan is typically associated with bacterial resistance to lysozyme, a muramidase that serves as a central component of innate immunity. Here, we report that the peptidoglycan of Bacillus anthracis, the etiological agent of anthrax, is O-acetylated and that, unusually, this modification is produced by two unrelated families of O-acetyltransferases. Also, in contrast to other bacteria, O-acetylation of B. anthracis peptidoglycan is combined with N-deacetylation to confer resistance of cells to lysozyme. Activity of the Pat O-acetyltransferases is required for the separation of the daughter cells following bacterial division and for anchoring of one of the major S-layer proteins. Our results indicate that peptidoglycan O-acetylation modulates endogenous muramidase activity affecting the cell-surface properties and morphology of this important pathogen.
Department of Microbiology and Immunology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.
Maria-Halima
MH
Laaberki
John
J
Pfeffer
Anthony J
AJ
Clarke
Jonathan
J
Dworkin
D000107:Acetylation; D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D001408:Bacillus anthracis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division / Q000502:physiology*; D024881:Drug Resistance, Bacterial / Q000235:genetics; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D009113:Muramidase / Q000494:pharmacology; D010457:Peptidoglycan / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; D010457:Peptidoglycan; C055764:S-layer proteins; D000123:Acetyltransferases; D009113:Muramidase