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Correlation between the structure of the bacterial peptidoglycan monomer unit, the specificity of transpeptidation, and susceptibility to beta-lactams.

Peptidoglycan is a continuous covalent macromolecular structure found on the outside of the cytoplasmic membrane of almost all bacteria and exclusively in these organisms. As the main structural component of the bacterial cell wall, its function is to preserve cell integrity by withstanding the internal osmotic pressure. It is also responsible for the maintenance of a defined cell shape, and it is intimately involved in the cell division process (1). The two basic structural features of this giant macromolecule are linear glycan chains interlinked with short peptide bridges. The glycan chains are composed of alternating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc). The carboxyl group of each N-acetylmuramic acid residue is substituted by a short stem peptide subunit. The formation of the three-dimensional network structure of peptidoglycan is ensured by cross-linking between the peptide subunit of one chain with that of a neighboring chain (2).