Structural variation in the glycan strands of bacterial peptidoglycan

Authors


  • Editor: Jacques Coyette

Correspondence: Waldemar Vollmer, Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle upon Tyne, Catherine Cookson Building, Framlington Place, Newcastle upon Tyne NE2 4HH, UK. Tel.: +44 0 191 222 6295; fax: +44 0 191 222 7424; e-mail: w.vollmer@ncl.ac.uk

Abstract

The normal, unmodified glycan strands of bacterial peptidoglycan consist of alternating residues of β-1,4-linked N-acetylmuramic acid and N-acetylglucosamine. In many species the glycan strands become modified after their insertion into the cell wall. This review describes the structure of secondary modifications and of attachment sites of surface polymers in the glycan strands of peptidoglycan. It also provides an overview of the occurrence of these modifications in various bacterial species. Recently, enzymes responsible for the N-deacetylation, N-glycolylation and O-acetylation of the glycan strands were identified. The presence of these modifications affects the hydrolysis of peptidoglycan and its enlargement during cell growth. Glycan strands are frequently deacetylated and/or O-acetylated in pathogenic species. These alterations affect the recognition of bacteria by host factors, and contribute to the resistance of bacteria to host defence factors such as lysozyme.

Ancillary