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Cited by 373

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Structural variation in the glycan strands of bacterial peptidoglycan

Open access
Vollmer, Waldemar·2008·FEMS Microbiology Reviews

Abstract

The normal, unmodified glycan strands of bacterial peptidoglycan consist of alternating residues of beta-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.

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Crossref · 10.1111/j.1574-6976.2007.00088.x

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Metadata

Authors
Vollmer, W.
Venue
FEMS Microbiology Reviews
Published
2008-03
Volume
32
Issue
2
Pages
287-306
ISSN
  • 0168-6445 (ISSN-L)
  • 1574-6976
OpenAlex
W2058127453
Cited by
373
References
4
FWCI
12.30
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Structural variation in the glycan strands of bacterial peptidoglycan. https://app.cochat.ai/papers/10.1111/j.1574-6976.2007.00088.x
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Vollmer, W. (2008). Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiology Reviews. https://doi.org/10.1111/j.1574-6976.2007.00088.x

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