Variability in the lipooligosaccharide structure and endotoxicity among Bordetella pertussis strains

J Infect Dis. 2010 Dec 15;202(12):1897-906. doi: 10.1086/657409. Epub 2010 Nov 4.


Bordetella endotoxins show remarkable structural variability both among each other and in comparison to other gram-negative bacteria. Here we demonstrate that, in contrast to the common Bordetella pertussis laboratory strain and Tohama I derivative BP338, lipooligosaccharide from mouse challenge strain 18-323 is a poor inducer of inflammatory cytokines in human and murine macrophages, is greatly impaired in Toll-like receptor 4-mediated activation of nuclear factor-κB in transfected HEK-293 cells, and functions as a Toll-like receptor 4 antagonist. Comparison of lipid A and lipooligosaccharide structures of B. pertussis strains BP338 and 18-323 revealed that 18-323 (1) lacks the ability to modify its lipid A phosphate groups with glucosamine, (2) is distinct in its acylation at the C3' position of the lipid A diglucosamine backbone, and (3) expresses molecular lipooligosaccharide species that lack a terminal heptose. Our findings have important implications for interpreting previous studies of host defenses to B. pertussis infection in mice and in vitro.

Publication types

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

MeSH terms

  • Animals
  • Bordetella pertussis / chemistry*
  • Bordetella pertussis / pathogenicity
  • Cell Line
  • Endotoxins / chemistry*
  • Endotoxins / toxicity*
  • Humans
  • Lipopolysaccharides / chemistry*
  • Lipopolysaccharides / toxicity*
  • Macrophages / drug effects
  • Macrophages / immunology
  • Mice
  • NF-kappa B / metabolism
  • Toll-Like Receptors / drug effects


  • Endotoxins
  • Lipopolysaccharides
  • NF-kappa B
  • Toll-Like Receptors
  • lipid-linked oligosaccharides