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

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 Lett

journal_title

FEBS letters

authors

Hasan S,Osickova A,Bumba L,Novák P,Sebo P,Osicka R

doi

10.1016/j.febslet.2014.12.023

subject

Has Abstract

pub_date

2015-01-30 00:00:00

pages

374-9

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(14)00903-X

journal_volume

589

pub_type

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