Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8329779 | International Journal of Biological Macromolecules | 2016 | 9 Pages |
Abstract
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 16Â kDa 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.
Keywords
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Authors
Nerry Tatiana CecÃlio, Fernanda Caroline Carvalho, Yan Liu, Martin Moncrieffe, PatrÃcia Andressa de Almeida Buranello, Andre Luiz Zorzetto-Fernandes, Douglas Dalle Luche, Ebert Seixas Hanna, Sandro Gomes Soares, Ten Feizi, Nicholas J. Gay,