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

Author(s):Show less -

Cecilio, Nerry Tatiana ^[1] ; Carvalho, Fernanda Caroline ^[1] ; Liu, Yan ^[2] ; Moncrieffe, Martin ^[3] ; de Almeida Buranello, Patricia Andressa ^[1] ; Zorzetto-Fernandes, Andre Luiz ^[1] ; Dalle Luche, Douglas ^[4] ; Hanna, Ebert Seixas ^[1] ; Soares, Sandro Gomes ^[1] ; Feizi, Ten ^[2] ; Gay, Nicholas J. ^[3] ; Goldman, Maria Helena S. ^[4] ; Roque-Barreira, Maria Cristina ^[1]

Affiliation

^[1] Univ Sao Paulo, Dept Biol Celular & Mol Bioagentes Patogen, Fac Med Ribeirao Preto, BR-14049900 Sao Paulo - Brazil

^[2] Univ London Imperial Coll Sci Technol & Med, Dept Med, Glycosci Lab, London - England

^[3] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW - England

^[4] Univ Sao Paulo, Dept Biol, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14049900 Sao Paulo - Brazil

• Document type: Journal article
• Source: International Journal of Biological Macromolecules; v. 82, p. 22-30, JAN 2016.
• Web of Science Citations: 5

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 n-mannose-binding lectin isolated from the seeds of jackfruit (Artocarpus heterophyllus), is composed of 16 kDa subunits that are associated to form a homotetramer. Native ArtinM (n-ArtinM) exerts immunomodulatoiy 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. (C) 2015 The Authors. Published by Elsevier B.V. (AU)

• FAPESP's process: 09/16146-9 - Induced cell activation by ArtinM: interference of the quaternary structure of different recombinant forms on neutrophil functions and interaction with glycosylated receptors on surface of these cells.
• Grantee: Nerry Tatiana Cecilio
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 13/04088-0 - Lectin from pathogens
• Grantee: Maria Cristina Roque Antunes Barreira
• Support Opportunities: Research Projects - Thematic Grants