Protein glycosylation in bacterial mucosal pathogens

Nat Rev Microbiol. 2005 Mar;3(3):225-37. doi: 10.1038/nrmicro1100.


In eukaryotes, glycosylated proteins are ubiquitous components of extracellular matrices and cellular surfaces. Their oligosaccharide moieties are implicated in a wide range of cell-cell and cell-matrix recognition events that are required for biological processes ranging from immune recognition to cancer development. Glycosylation was previously considered to be restricted to eukaryotes; however, through advances in analytical methods and genome sequencing, there have been increasing reports of both O-linked and N-linked protein glycosylation pathways in bacteria, particularly amongst mucosal-associated pathogens. Studying glycosylation in relatively less-complicated bacterial systems provides the opportunity to elucidate and exploit glycoprotein biosynthetic pathways. We will review the genetic organization, glycan structures and function of glycosylation systems in mucosal bacterial pathogens, and speculate on how this knowledge may help us to understand glycosylation processes in more complex eukaryotic systems and how it can be used for glycoengineering.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / pathogenicity*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / physiology
  • Campylobacter jejuni / metabolism
  • Campylobacter jejuni / pathogenicity
  • Glycoproteins / genetics
  • Glycoproteins / physiology*
  • Glycosylation
  • Glycosyltransferases / physiology
  • Mucous Membrane / microbiology*


  • Bacterial Proteins
  • Glycoproteins
  • Glycosyltransferases