Yeast expressed ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM
| العنوان: | Yeast expressed ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM |
|---|---|
| المؤلفون: | Nerry Tatiana Cecílio, Fernanda Caroline Carvalho, Yan Liu, Martin Moncrieffe, Patrícia Andressa de Almeida Buranello, Andre Luiz Zorzetto-Fernandes, Douglas Dalle Luche, Ebert Seixas Hanna, Sandro Gomes Soares, Ten Feizi, Nicholas J. Gay, Maria Helena S. Goldman, Maria Cristina Roque-Barreira |
| المساهمون: | Engineering & Physical Science Research Council (E, Wellcome Trust |
| المصدر: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| بيانات النشر: | Elsevier, 2015. |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | Male, 0301 basic medicine, Neutrophils, KM+, Polymers, Biochemistry, Cell Degranulation, law.invention, ACTIVATION, Mice, ArtinM, Cell Movement, Structural Biology, law, Yeasts, INFECTION, Immunomodulatory lectins, FÁRMACOS, Mast Cells, SPECIFICITY, Mannan-binding lectin, Recombinant proteins, ARTOCARPUS-INTEGRIFOLIA SEEDS, Molecular Structure, biology, Glycobiology, Chemistry, Degranulation, General Medicine, Chemistry, Applied, Physical Sciences, Recombinant DNA, Cytokines, MAST-CELLS, KM PLUS, Life Sciences & Biomedicine, Protein Binding, Homotetramer, Biochemistry & Molecular Biology, Saccharomyces cerevisiae, Carbohydrates, Polymer Science, BETA, 03 medical and health sciences, Polysaccharides, MANNOSE-BINDING LECTIN, Animals, Humans, Molecular Biology, Science & Technology, RECEPTOR, Hemagglutination, Macrophages, Lectin, 0601 Biochemistry And Cell Biology, biology.organism_classification, Toll-Like Receptor 2, Yeast, Mannose-Binding Lectins, 030104 developmental biology, biology.protein |
| الوصف: | 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. |
| اللغة: | English |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c665abe345abdbc0a6b502ab31719d0 http://hdl.handle.net/10044/1/32572 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....8c665abe345abdbc0a6b502ab31719d0 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |