Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hasan S,Osickova A,Bumba L,Novák P,Sebo P,Osicka Rdoi
10.1016/j.febslet.2014.12.023subject
Has Abstractpub_date
2015-01-30 00:00:00pages
374-9issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00903-Xjournal_volume
589pub_type
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