Lectin domains in the toxin of Bordetella pertussis: selectin mimicry linked to microbial pathogenesis

Jens Sandros, Eva Rozdzinski, Jie Zheng, David Cowburn, Elaine Tuomanen

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

The pathogenesis of many infectious diseases is critically determined by prokaryotic lectins which enable differential recognition and activation of targeted eukaryotic cells. Some bacterial adhesins mimic and co-opt eukaryotic cell-cell adhesion motifs. This is illustrated by the toxin of Bordetella pertussis. Pertussis toxin mediates intoxication of eukaryotic cells by elevation of cAMP and it serves as an adhesin binding the bacteria to ciliated cells and respiratory macrophages. These activities are mediated by the lectin-like properties of the binding oligomer of the toxin. A comparison of pertussis toxin and the selectins involved in leukocyte trafficking indicates that these prokaryotic and eukaryotic C-type lectins share some element of primary sequence similarity, three dimensional structure, and biological activities. Such mimicry suggests a link between eukaryotic cell-cell adhesion motifs and microbial pathogenesis.

Original languageEnglish (US)
Pages (from-to)501-506
Number of pages6
JournalGlycoconjugate Journal
Volume11
Issue number6
DOIs
StatePublished - Dec 1 1994
Externally publishedYes

Keywords

  • adherence
  • fibronectin
  • microbial pathogenesis
  • pertussis
  • selectin
  • toxin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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