Details

Autor(en) / Beteiligte

• Hasan, Shakir
• Osickova, Adriana
• Bumba, Ladislav
• Novák, Petr
• Sebo, Peter
• Osicka, Radim

Titel

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

Ist Teil von

• FEBS letters, 2015-01, Vol.589 (3), p.374-379

Ort / Verlag

England: Elsevier B.V

Erscheinungsjahr

2015

Link zum Volltext

Quelle

Wiley Online Library Journals Frontfile Complete

Beschreibungen/Notizen

• •CR3 (CD11b/CD18) is glycosylated at the majority of predicted N-glycosylation sites.•A set of 25 CR3 mutant variants lacking individual N-glycans was generated.•The importance of individual N-glycans in interaction of CR3 with CyaA was explored.•N-glycans at the C-terminus of CD11b were involved in binding and cytotoxic activity of CyaA. 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.