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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10319363" target="_blank" >RIV/00216208:11310/15:10319363 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/15:00444555

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.febslet.2014.12.023" target="_blank" >http://dx.doi.org/10.1016/j.febslet.2014.12.023</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.febslet.2014.12.023" target="_blank" >10.1016/j.febslet.2014.12.023</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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, enhancingboth affinity and specificity of the integrin-toxin interaction. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    FEBS Letters

  • ISSN

    0014-5793

  • e-ISSN

  • Volume of the periodical

    589

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    6

  • Pages from-to

    374-379

  • UT code for WoS article

    000349403300013

  • EID of the result in the Scopus database

    2-s2.0-84921509836