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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,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1968 do 2015
Wiley Free Content
od 1997 do Před 1 rokem
- MeSH
- adenylátcyklasový toxin genetika metabolismus MeSH
- antigeny CD11b chemie metabolismus MeSH
- antigeny CD18 chemie metabolismus MeSH
- asparagin genetika MeSH
- Bordetella pertussis metabolismus patogenita MeSH
- glutamin genetika MeSH
- glykosylace MeSH
- lidé MeSH
- makrofágový antigen 1 genetika metabolismus MeSH
- polysacharidy metabolismus MeSH
- substituce aminokyselin MeSH
- terciární struktura proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem 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.
Citace poskytuje Crossref.org
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