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Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding
S. Hasan, A. Osickova, L. Bumba, P. Novák, P. Sebo, R. Osicka,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 1968 to 2015
Wiley Free Content
from 1997 to 1 year ago
- MeSH
- Adenylate Cyclase Toxin genetics metabolism MeSH
- CD11b Antigen chemistry metabolism MeSH
- CD18 Antigens chemistry metabolism MeSH
- Asparagine genetics MeSH
- Bordetella pertussis metabolism pathogenicity MeSH
- Glutamine genetics MeSH
- Glycosylation MeSH
- Humans MeSH
- Macrophage-1 Antigen genetics metabolism MeSH
- Polysaccharides metabolism MeSH
- Amino Acid Substitution MeSH
- Protein Structure, Tertiary MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
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