Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells

Abstract Several plant lectins, or carbohydrate-binding proteins, interact with glycan moieties on the surface of immune cells, thereby influencing the immune response of these cells. Orysata, a mannose-binding lectin from rice, has been reported to exert immunomodulatory activities on insect cells....

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Pengyu Chen, Kristof De Schutter, Sonia Serna, Simin Chen, Qun Yang, Niels-Christian Reichardt, Els J. M. Van Damme, Guy Smagghe
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/99d59370bea94a8b9221e09bc016effa
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:99d59370bea94a8b9221e09bc016effa
record_format	dspace
spelling	oai:doaj.org-article:99d59370bea94a8b9221e09bc016effa2021-12-02T17:41:18ZGlycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells10.1038/s41598-021-97161-22045-2322https://doaj.org/article/99d59370bea94a8b9221e09bc016effa2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-97161-2https://doaj.org/toc/2045-2322Abstract Several plant lectins, or carbohydrate-binding proteins, interact with glycan moieties on the surface of immune cells, thereby influencing the immune response of these cells. Orysata, a mannose-binding lectin from rice, has been reported to exert immunomodulatory activities on insect cells. While the natural lectin is non-glycosylated, recombinant Orysata produced in the yeast Pichia pastoris (YOry) is modified with a hyper-mannosylated N-glycan. Since it is unclear whether this glycosylation can affect the YOry activity, non-glycosylated rOrysata was produced in Escherichia coli (BOry). In a comparative analysis, both recombinant Orysata proteins were tested for their carbohydrate specificity on a glycan array, followed by the investigation of the carbohydrate-dependent agglutination of red blood cells (RBCs) and the carbohydrate-independent immune responses in Drosophila melanogaster S2 cells. Although YOry and BOry showed a similar carbohydrate-binding profiles, lower concentration of BOry were sufficient for the agglutination of RBCs and BOry induced stronger immune responses in S2 cells. The data are discussed in relation to different hypotheses explaining the weaker responses of glycosylated YOry. In conclusion, these observations contribute to the understanding how post-translational modification can affect protein function, and provide guidance in the selection of the proper expression system for the recombinant production of lectins.Pengyu ChenKristof De SchutterSonia SernaSimin ChenQun YangNiels-Christian ReichardtEls J. M. Van DammeGuy SmaggheNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Pengyu Chen Kristof De Schutter Sonia Serna Simin Chen Qun Yang Niels-Christian Reichardt Els J. M. Van Damme Guy Smagghe Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells
description	Abstract Several plant lectins, or carbohydrate-binding proteins, interact with glycan moieties on the surface of immune cells, thereby influencing the immune response of these cells. Orysata, a mannose-binding lectin from rice, has been reported to exert immunomodulatory activities on insect cells. While the natural lectin is non-glycosylated, recombinant Orysata produced in the yeast Pichia pastoris (YOry) is modified with a hyper-mannosylated N-glycan. Since it is unclear whether this glycosylation can affect the YOry activity, non-glycosylated rOrysata was produced in Escherichia coli (BOry). In a comparative analysis, both recombinant Orysata proteins were tested for their carbohydrate specificity on a glycan array, followed by the investigation of the carbohydrate-dependent agglutination of red blood cells (RBCs) and the carbohydrate-independent immune responses in Drosophila melanogaster S2 cells. Although YOry and BOry showed a similar carbohydrate-binding profiles, lower concentration of BOry were sufficient for the agglutination of RBCs and BOry induced stronger immune responses in S2 cells. The data are discussed in relation to different hypotheses explaining the weaker responses of glycosylated YOry. In conclusion, these observations contribute to the understanding how post-translational modification can affect protein function, and provide guidance in the selection of the proper expression system for the recombinant production of lectins.
format	article
author	Pengyu Chen Kristof De Schutter Sonia Serna Simin Chen Qun Yang Niels-Christian Reichardt Els J. M. Van Damme Guy Smagghe
author_facet	Pengyu Chen Kristof De Schutter Sonia Serna Simin Chen Qun Yang Niels-Christian Reichardt Els J. M. Van Damme Guy Smagghe
author_sort	Pengyu Chen
title	Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells
title_short	Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells
title_full	Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells
title_fullStr	Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells
title_full_unstemmed	Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells
title_sort	glycosylation reduces the glycan-independent immunomodulatory effect of recombinant orysata lectin in drosophila s2 cells
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/99d59370bea94a8b9221e09bc016effa
work_keys_str_mv	AT pengyuchen glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT kristofdeschutter glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT soniaserna glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT siminchen glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT qunyang glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT nielschristianreichardt glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT elsjmvandamme glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells AT guysmagghe glycosylationreducestheglycanindependentimmunomodulatoryeffectofrecombinantorysatalectinindrosophilas2cells
_version_	1718379718897565696

Glycosylation reduces the glycan-independent immunomodulatory effect of recombinant Orysata lectin in Drosophila S2 cells

Ejemplares similares