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.
- MeSH
- adenylátcyklasový toxin genetika metabolismus MeSH
- antigeny CD11b chemie metabolismus MeSH
- antigeny CD18 chemie metabolismus MeSH
- asparagin genetika MeSH
- Bordetella pertussis metabolismus patogenita MeSH
- glutamin genetika MeSH
- glykosylace MeSH
- lidé MeSH
- makrofágový antigen 1 genetika metabolismus MeSH
- polysacharidy metabolismus MeSH
- substituce aminokyselin MeSH
- terciární struktura proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
