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O-Acetylation of peptidoglycan is required for proper cell separation and S-layer anchoring in Bacillus anthracis

Maria-Halima Laaberki1, John Pfeffer, Anthony J Clarke

  • 1Department of Microbiology and Immunology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.

The Journal of Biological Chemistry
|December 8, 2010
PubMed

Insights

Bacillus anthracis peptidoglycan O-acetylation, unusual in its dual enzyme source and combined N-deacetylation, confers lysozyme resistance. This modification impacts cell division and S-layer protein anchoring in the anthrax pathogen.

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Innate Immunity

Background:

  • O-acetylation of peptidoglycan typically confers bacterial resistance to lysozyme, a key innate immunity enzyme.
  • Lysozyme degrades peptidoglycan, a crucial component of the bacterial cell wall.

Purpose of the Study:

  • To investigate the O-acetylation of peptidoglycan in Bacillus anthracis, the causative agent of anthrax.
  • To elucidate the enzymes responsible for O-acetylation and their role in bacterial resistance and cell surface properties.

Main Methods:

  • Analysis of peptidoglycan composition in Bacillus anthracis.
  • Identification and characterization of O-acetyltransferase enzymes.
  • Assessment of bacterial resistance to lysozyme.
  • Evaluation of cell division and S-layer protein anchoring.

Main Results:

  • Bacillus anthracis peptidoglycan is O-acetylated by two unrelated O-acetyltransferase families.
  • O-acetylation, combined with N-deacetylation, confers resistance to lysozyme.
  • Pat O-acetyltransferases are essential for daughter cell separation and S-layer protein anchoring.

Conclusions:

  • Peptidoglycan O-acetylation in Bacillus anthracis is a unique process with implications for lysozyme resistance.
  • This modification influences bacterial cell division and surface architecture.
  • O-acetylation modulates endogenous muramidase activity, affecting the pathogen's cell-surface properties and morphology.

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