N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL

Cell Microbiol. 2009 Dec;11(12):1768-81. doi: 10.1111/j.1462-5822.2009.01370.x. Epub 2009 Aug 13.


An increasing number of bacterial pathogens produce an array of glycoproteins of unknown function. Here we report that Campylobacter jejuni proteins that are modified by the N-linked glycosylation machinery encoded by the pgl locus bind the human Macrophage Galactose-type lectin (MGL). MGL receptor binding was abrogated by EDTA and N-acetylgalactosamine (GalNAc) and was successfully transferred to Escherichia coli by introducing the C. jejuni pgl locus together with a glycan acceptor protein. In addition to glycoproteins, C. jejuni lipooligosaccharide with a terminal GalNAc residue was recognized by MGL. Recombinant E. coli expressing the C. jejuni pgl locus in the absence of a suitable glycan acceptor protein produced altered lipopolysaccharide glycoforms that gained MGL reactivity. Infection assays demonstrated high levels of GalNAc-dependent interaction of the recombinant E. coli with MGL-transfected mammalian cells. In addition, interleukin-6 production by human dendritic cells was enhanced by C. jejuni lacking N-linked glycans compared with wild-type bacteria. Collectively, our results provide evidence that both N-linked glycoproteins and distinct lipooligosaccharide glycoforms of C. jejuni are ligands for the human C-type lectin MGL and that the C. jejuni N-glycosylation machinery can be exploited to target recombinant bacteria to MGL-expressing eukaryotic cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylgalactosamine / metabolism
  • Acetylgalactosamine / pharmacology
  • Animals
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • CHO Cells
  • Campylobacter Infections / metabolism*
  • Campylobacter Infections / microbiology
  • Campylobacter jejuni / drug effects
  • Campylobacter jejuni / genetics
  • Campylobacter jejuni / metabolism*
  • Chelating Agents / pharmacology
  • Cricetinae
  • Cricetulus
  • Dendritic Cells / metabolism
  • Edetic Acid / pharmacology
  • Escherichia coli / metabolism
  • Glycoproteins / metabolism*
  • Glycosylation
  • Host-Pathogen Interactions / drug effects
  • Humans
  • Interleukin-6 / biosynthesis
  • Lectins, C-Type / metabolism*
  • Lipopolysaccharides / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Substrate Specificity


  • Bacterial Proteins
  • Chelating Agents
  • Glycoproteins
  • Interleukin-6
  • Lectins, C-Type
  • Lipopolysaccharides
  • MGL lectin, human
  • Recombinant Proteins
  • lipid-linked oligosaccharides
  • Edetic Acid
  • Acetylgalactosamine