Effect of purification of galactooligosaccharides derived from lactulose with Saccharomyces cerevisiae on their capacity to bind immune cell receptor Dectin-2
Autor: | Mar Villamiel, Agustín Olano, Norihito Kawasaki, Antonia Montilla, Alexandra Wittmann, Ian D. Young |
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Přispěvatelé: | Ministerio de Economía y Competitividad (España), CSIC - Centro Nacional de Biotecnología (CNB), Comunidad de Madrid, Biotechnology and Biological Sciences Research Council (UK), European Commission |
Jazyk: | angličtina |
Rok vydání: | 2019 |
Předmět: |
Proteomics
030309 nutrition & dietetics Saccharomyces cerevisiae Mutant Oligosaccharides Polysaccharide Saccharomyces Fungal Proteins 03 medical and health sciences 0404 agricultural biotechnology Bioassay Lectins C-Type Receptors Immunologic Receptor Mannoproteins 2. Zero hunger chemistry.chemical_classification 0303 health sciences Innate immune system biology Biological activity 04 agricultural and veterinary sciences biology.organism_classification 040401 food science Lactulose 3. Good health Prebiotics chemistry Biochemistry Food Science Dectin-2 |
Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
Popis: | Lactulose-derived oligosaccharides (OsLu) are prebiotic galactooligosaccharides (GOS) beneficial for human health including immunomodulatory properties; however, the molecular mechanism is unclear. OsLu produced by enzymatic synthesis can be purified with Saccharomyces cerevisiae (OsLu-Sc). We show that this purification introduces yeast-derived proteins reactive to Dectin-2, an innate immune receptor for fungal polysaccharides. Using a cell-based bioassay, we tested the binding of OsLu and GOS samples to Dectin-2. While OsLu purified with active charcoal and commercial GOS failed to bind to Dectin-2, we found OsLu-Sc bound to this receptor. The carbohydrate-binding incompetent mutant of Dectin-2 failed to bind to OsLu-Sc. These data suggest that OsLu-Sc introduced carbohydrate ligands for Dectin-2. In accordance with this, proteomic analysis revealed OsLu-Sc contained S. cerevisiae-derived mannoproteins. Therefore, our data highlight the importance of the purification method for OsLu, which may positively affect the bioactivity of OsLu. Data are available via ProteomeXchange with identifier PXD010495. The proteomic analysis was performed in the Proteomics Facility of The Spanish National Center for Biotechnology (CNB-CSIC) that belongs to ProteoRed, PRB2-ISCIII, supported by grant PT13/0001. Authors thank J. Megino, S. Garrido, N. E. Nogués, and T. Moufle-Milot for technical assistance. This work has been funded by MINECO of Spain Project AGL2014-53445-R, ALIBIRD-CM S-2013/ABI-2728. This work was also supported by the Biotechnology and Biological Sciences Research Council (BBSRC) Institute Strategic Programme for Food and Health (Project ID: BBS/E/F/00044486). NK would like to thank the Marie-Curie International Incoming Fellowship from the European Union 7th Framework Programme (Project ID: 628043). IDY would like to thank BBSRC doctoral training partnership program grant (Project ID: BB/J014524/1) and MV thanks Salvador de Madariaga Program from MINECO (Spain). |
Databáze: | OpenAIRE |
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