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Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding
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SYSNO ASEP 0444555 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding Author(s) Hasan, Shakir (MBU-M)
Osičková, Adriana (MBU-M) RID, ORCID
Bumba, Ladislav (MBU-M) RID, ORCID
Novák, Petr (MBU-M) RID, ORCID
Šebo, Peter (MBU-M) RID, ORCID
Osička, Radim (MBU-M) RID, ORCIDSource Title FEBS Letters. - : Wiley - ISSN 0014-5793
Roč. 589, č. 3 (2015), s. 374-379Number of pages 6 s. Language eng - English Country NL - Netherlands Keywords Adenylate cyclase toxin ; CD11b/CD18 ; Complement receptor type 3 Subject RIV CE - Biochemistry R&D Projects GAP302/11/0580 GA ČR - Czech Science Foundation (CSF) GA15-09157S GA ČR - Czech Science Foundation (CSF) GA15-11851S GA ČR - Czech Science Foundation (CSF) Institutional support MBU-M - RVO:61388971 UT WOS 000349403300013 DOI 10.1016/j.febslet.2014.12.023 Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2016
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