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

0444555 - MBÚ 2016 RIV NL eng J - Journal Article
Hasan, Shakir - Osičková, Adriana - Bumba, Ladislav - Novák, Petr - Šebo, Peter - Osička, Radim
Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding.
FEBS Letters. Roč. 589, č. 3 (2015), s. 374-379. ISSN 0014-5793. E-ISSN 1873-3468
R&D Projects: GA ČR(CZ) GAP302/11/0580; GA ČR(CZ) GA15-09157S; GA ČR(CZ) GA15-11851S
Institutional support: RVO:61388971
Keywords : Adenylate cyclase toxin * CD11b/CD18 * Complement receptor type 3
Subject RIV: CE - Biochemistry
Impact factor: 3.519, year: 2015

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.
Permanent Link: http://hdl.handle.net/11104/0247065