Yeast expressed ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM

Recent advances in glycobiology have revealed the essential role of lectins in deciphering the glycocodes at the cell surface to generate important biological signaling responses. ArtinM, a d-mannose-binding lectin isolated from the seeds of jackfruit (Artocarpus heterophyllus), is composed of 16kDa...

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Bibliographic Details
Published in:	International journal of biological macromolecules Vol. 82; pp. 22 - 30
Main Authors:	Cecílio, Nerry Tatiana, Carvalho, Fernanda Caroline, Liu, Yan, Moncrieffe, Martin, Buranello, Patrícia Andressa de Almeida, Zorzetto-Fernandes, Andre Luiz, Luche, Douglas Dalle, Hanna, Ebert Seixas, Soares, Sandro Gomes, Feizi, Ten, Gay, Nicholas J., Goldman, Maria Helena S., Roque-Barreira, Maria Cristina
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier B.V 01-01-2016
Subjects:	Animals ArtinM Carbohydrates - chemistry Cell Degranulation - drug effects Cell Degranulation - immunology Cell Movement - drug effects Cell Movement - immunology Cytokines - biosynthesis Hemagglutination Humans Immunomodulatory lectins Macrophages - drug effects Macrophages - immunology Macrophages - metabolism Male Mannose-Binding Lectins - chemistry Mannose-Binding Lectins - metabolism Mannose-Binding Lectins - pharmacology Mast Cells - drug effects Mast Cells - immunology Mast Cells - metabolism Mice Molecular Structure Neutrophils - drug effects Neutrophils - immunology Neutrophils - metabolism Polysaccharides - chemistry Protein Binding Recombinant Proteins Toll-Like Receptor 2 Yeasts - genetics Yeasts - metabolism Immunomodulatory lectins Recombinant proteins ArtinM
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Summary:	Recent advances in glycobiology have revealed the essential role of lectins in deciphering the glycocodes at the cell surface to generate important biological signaling responses. ArtinM, a d-mannose-binding lectin isolated from the seeds of jackfruit (Artocarpus heterophyllus), is composed of 16kDa subunits that are associated to form a homotetramer. Native ArtinM (n-ArtinM) exerts immunomodulatory and regenerative effects, but the potential pharmaceutical applicability of the lectin is highly limited by the fact that its production is expensive, laborious, and impossible to be scaled up. This led us to characterize a recombinant form of the lectin obtained by expression in Saccharomyces cerevisiae (y-ArtinM). In the present study, we demonstrated that y-ArtinM is similar to n-ArtinM in subunit arrangement, oligomerization and carbohydrate binding specificity. We showed that y-ArtinM can exert n-ArtinM biological activities such as erythrocyte agglutination, stimulation of neutrophil migration and degranulation, mast cell degranulation, and induction of interleukin-12 and interleukin-10 production by macrophages. In summary, the expression of ArtinM in yeast resulted in successful production of an active, recombinant form of ArtinM that is potentially useful for pharmaceutical application.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0141-8130 1879-0003
DOI:	10.1016/j.ijbiomac.2015.09.062