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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00444555

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

FEBS Letters

ISSN

0014-5793

e-ISSN

—

Svazek periodika

589

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

374-379

Kód UT WoS článku

000349403300013

EID výsledku v databázi Scopus

2-s2.0-84921509836