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Lookup NU author(s): Professor Waldemar Vollmer
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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. © 2007 Federation of European Microbiological Societies.
Author(s): Vollmer W
Publication type: Article
Publication status: Published
Journal: FEMS Microbiology Reviews
ISSN (print): 0168-6445
ISSN (electronic): 1574-6976
Publisher: Wiley-Blackwell Publishing Ltd.
PubMed id: 18070068
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