Differential binding of lectins IL-2 and CSL to candida albicans and cancer cells

Glycobiology
J P ZanettaJ C Michalski

Abstract

The demonstration that interleukin 2 (IL-2) is a lectin specific for oligomannosides allows to understand a new function for this cytokine: as a bifunctional molecule when bound to its receptor ss, IL-2 associates the latter which the CD3/TCR complex, interacting with oligosaccharides of CD3 through its carbohydrate-recognition domain (Zanetta et al. , 1996, Biochem. J., 318, 49-53). This induces the tyrosine phosphorylation of the IL-2R beta by ++p56(lck) , the first step of the IL-2-dependent signaling. Since this specific association is disrupted in vitro by oligomannosides with five and six mannose residues, we made the hypothesis that pathogenic cells or microorganisms could bind IL-2, consequently disturbing the IL-2-dependent response. This study shows that the pathogenic yeast Candida albicans (in contrast with nonpathogenic yeasts) binds high amounts of IL-2 as did cancer cells. In contrast with cancer cells, yeasts do not bind the Man6GlcNAc2-specific lectin CSL, an endogenous "amplifier of activation signals" (Zanetta et al. , 1995, Biochem. J., 311, 629-636).

Citations

Sep 12, 2002·Biochimica Et Biophysica Acta·Christelle CeboJean-Pierre Zanetta
Jul 25, 2008·Orphanet Journal of Rare Diseases·Dag Malm, Øivind Nilssen
Nov 26, 1998·Biotechnic & Histochemistry : Official Publication of the Biological Stain Commission·H J GabiusK Kayser
Jan 15, 2002·The Journal of Biological Chemistry·Christelle CeboJean-Pierre Zanetta
Aug 12, 2010·Clinical and Applied Thrombosis/hemostasis : Official Journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis·Jasmina AhluwaliaNeelam Varma
Jan 8, 1999·Biochimica Et Biophysica Acta·T R Gemmill, R B Trimble

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