Determination of the structure of the O-antigen and the lipid A from the entomopathogenic bacterium Pseudomonas entomophila lipopolysaccharide along with its immunological properties

Carbohydr Res. 2015 Aug 14:412:20-7. doi: 10.1016/j.carres.2015.04.017. Epub 2015 May 1.

Abstract

The structure and the immunology of the lipopolysaccharide (LPS) of Pseudomonas entomophila, an entomopathogenic bacterium isolated from the fruit fly Drosophila melanogaster, was characterized. The O-antigen portion was established and resulted to be built up of a repetitive unit constituted by four monosaccharide residues, all L configured, all deoxy at C-6 and with an acetamido function at C-2: →3)-α-l-FucNAc-(1→4)-α-l-FucNAc-(1→3)-α-l-FucNAc-(1→3)-β-l-QuiNAc-(1→ The structural analysis of lipid A, showed a mixture of different species. The diphosphorylated glucosamine backbone carries six fatty acids consistent with the composition C10:0 3(OH), C12:0 2(OH) and C12:0 3(OH), whereas other species differs by the number of phosphates and/or of fatty acids. The immunology experiments demonstrated that the LPS structure of P. entomophila displayed a low ability to engage the TLR4-mediated signaling correlated to a significant antagonistic activity toward hexa-acylated LPS structures.

Keywords: Drosophila melanogaster; Innate immunity; Lipopolysaccharide; Pseudomonas entomophila; Structural analysis.

MeSH terms

  • Animals
  • Drosophila melanogaster / immunology
  • Drosophila melanogaster / microbiology
  • Escherichia coli
  • Fatty Acids / chemistry
  • Humans
  • Lipid A / chemistry*
  • Lipid A / immunology
  • Lipopolysaccharides / chemistry*
  • Lipopolysaccharides / immunology
  • Macrophages / immunology
  • Macrophages / metabolism
  • O Antigens / chemistry*
  • O Antigens / immunology
  • Pseudomonas / chemistry*
  • Pseudomonas / immunology
  • Pseudomonas / pathogenicity
  • Toll-Like Receptor 4 / immunology
  • Toll-Like Receptor 4 / metabolism

Substances

  • Fatty Acids
  • Lipid A
  • Lipopolysaccharides
  • O Antigens
  • TLR4 protein, human
  • Toll-Like Receptor 4