Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM

Autor(es)

Liu, Y. ^[1] ; Cecilio, N. T. ^[2] ; Carvalho, F. C. ^[2] ; Roque-Barreira, M. C. ^[2] ; Feizi, T. ^[1]

Afiliação do(s) autor(es)

^[1] Imperial Coll London, Dept Med, Glycosci Lab, London - England

^[2] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogen, Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: DATA IN BRIEF; v. 5, p. 1035-1047, DEC 2015.
• Citações Web of Science: 5

Resumo

This article contains data related to the researc.h article entitled ``Yeast-derived ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM{''} by Cecilio et al. (2015) {[}1] ArtinM, a D-mannose-binding lectin isolated from the seeds of Artocarpus heterophyllus, exerts immunomodulatory and regenerative activities through its Carbohydrate Recognition Domain (CRD) (Souza et al., 2013; Mariano et al., 2014 {[}2,3]). The limited availability of the native lectin (n-ArtinM) led us to characterize a recombinant form of the protein, obtained by expression in Saccharomyces cerevisiae (y-ArtinM). We compared the carbohydrate binding specificities of y-ArtinM and n-ArtinM by analyzing the binding of biotinylated preparations of the two lectin forms using a neoglycolipid (NGL)-based glycan microarray. Data showed that y-ArtinM mirrored the specificity exhibited by n-ArtinM. (C) 2015 The Authors. Published by Elsevier Inc. (AU)

• Processo FAPESP: 09/16146-9 - Ativação celular induzida por ArtinM: interferência da estrutura quaternária das diferentes formas recombinantes sobre funções de neutrófilos e interação com receptores glicosilados da superfície dessas células.
• Beneficiário: Nerry Tatiana Cecilio
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 13/04088-0 - Lectinas de patógenos
• Beneficiário: Maria Cristina Roque Antunes Barreira
• Modalidade de apoio: Auxílio à Pesquisa - Temático