Bacterial cell-wall recycling

Ann N Y Acad Sci. 2013 Jan;1277(1):54-75. doi: 10.1111/j.1749-6632.2012.06813.x. Epub 2012 Nov 16.

Abstract

Many Gram-negative and Gram-positive bacteria recycle a significant proportion of the peptidoglycan components of their cell walls during their growth and septation. In many--and quite possibly all--bacteria, the peptidoglycan fragments are recovered and recycled. Although cell-wall recycling is beneficial for the recovery of resources, it also serves as a mechanism to detect cell-wall-targeting antibiotics and to regulate resistance mechanisms. In several Gram-negative pathogens, anhydro-MurNAc-peptide cell-wall fragments regulate AmpC β-lactamase induction. In some Gram-positive organisms, short peptides derived from the cell wall regulate the induction of both β-lactamase and β-lactam-resistant penicillin-binding proteins. The involvement of peptidoglycan recycling with resistance regulation suggests that inhibitors of the enzymes involved in the recycling might synergize with cell-wall-targeted antibiotics. Indeed, such inhibitors improve the potency of β-lactams in vitro against inducible AmpC β-lactamase-producing bacteria. We describe the key steps of cell-wall remodeling and recycling, the regulation of resistance mechanisms by cell-wall recycling, and recent advances toward the discovery of cell-wall-recycling inhibitors.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Bacteria / chemistry
  • Bacteria / metabolism*
  • Bacterial Proteins / metabolism
  • Cell Wall / chemistry
  • Cell Wall / metabolism*
  • Glycosyltransferases / metabolism
  • Gram-Negative Bacteria / chemistry
  • Gram-Negative Bacteria / metabolism
  • Gram-Positive Bacteria / chemistry
  • Gram-Positive Bacteria / metabolism
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism
  • Penicillin-Binding Proteins / metabolism
  • Peptidoglycan / metabolism
  • Protein Binding
  • beta-Lactamases / metabolism

Substances

  • Bacterial Proteins
  • Penicillin-Binding Proteins
  • Peptidoglycan
  • AmpR protein, Bacteria
  • Glycosyltransferases
  • N-Acetylmuramoyl-L-alanine Amidase
  • AmpC beta-lactamases
  • beta-Lactamases