Journal
FEBS LETTERS
Volume 589, Issue 3, Pages 374-379Publisher
WILEY
DOI: 10.1016/j.febslet.2014.12.023
Keywords
Adenylate cyclase toxin; CD11b/CD18; Complement receptor type 3; N-linked glycosylation; Point mutants; Repeats in toxin
Funding
- Czech Science Foundation [GAP302/11/0580, 15-09157S, 15-11851S]
- Institute of Microbiology [RVO 61388971]
- Charles University in Prague [UNCE204025/2012]
Ask authors/readers for more resources
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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available