Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding

FEBS Lett. 2015 Jan 30;589(3):374-9. doi: 10.1016/j.febslet.2014.12.023. Epub 2014 Dec 29.


The interaction of Bordetella pertussis adenylate cyclase toxin (CyaA) with complement receptor 3 (CR3, CD11b/CD18) involves N-linked oligosaccharide chains. To investigate the relative importance of the individual N-glycans of CR3 for toxin activity, the asparagine residues of the consensus N-glycosylation sites of CR3 were substituted with glutamine residues that cannot be glycosylated. Examination of CR3 mutant variants and mass spectrometry analysis of the N-glycosylation pattern of CR3 revealed that N-glycans located in the C-terminal part of the CD11b subunit are involved in binding and cytotoxic activity of CyaA. We suggest that these N-glycans form a defined clustered saccharide patch that enables multivalent contact of CR3 with CyaA, enhancing both affinity and specificity of the integrin-toxin interaction.

Keywords: Adenylate cyclase toxin; CD11b/CD18; Complement receptor type 3; N-linked glycosylation; Point mutants; Repeats in toxin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylate Cyclase Toxin / genetics
  • Adenylate Cyclase Toxin / metabolism*
  • Amino Acid Substitution
  • Asparagine / genetics
  • Bordetella pertussis / metabolism
  • Bordetella pertussis / pathogenicity
  • CD11b Antigen / chemistry
  • CD11b Antigen / metabolism*
  • CD18 Antigens / chemistry
  • CD18 Antigens / metabolism*
  • Glutamine / genetics
  • Glycosylation
  • Humans
  • Macrophage-1 Antigen / genetics
  • Macrophage-1 Antigen / metabolism*
  • Polysaccharides / metabolism*
  • Protein Structure, Tertiary


  • Adenylate Cyclase Toxin
  • CD11b Antigen
  • CD18 Antigens
  • Macrophage-1 Antigen
  • Polysaccharides
  • Glutamine
  • Asparagine