Variability in the lipooligosaccharide structure and endotoxicity among Bordetella pertussis strains

Nico Marr, Alexey Novikov, Adeline M. Hajjar, Martine Caroff, Rachel C. Fernandez

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23 Citations (Scopus)

Abstract

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 Tolllike receptor 4-mediated activation of nuclear factor-κB in transfected HEK-293 cells, and functions as a Tolllike 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.

Original languageEnglish
Pages (from-to)1897-1906
Number of pages10
JournalJournal of Infectious Diseases
Volume202
Issue number12
DOIs
Publication statusPublished - 15 Dec 2010
Externally publishedYes

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ASJC Scopus subject areas

  • Infectious Diseases
  • Immunology and Allergy

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