Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM
File(s)
Published version
Author(s)
Liu, Y
Cecilio, NT
Carvalho, FC
Roque Barreira, MC
Feizi, T
Type
Journal Article
Abstract
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 Cecílio 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] and [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.
Date Issued
2015-11-18
Date Acceptance
2015-11-08
Citation
Data in Brief, 2015, 5, pp.1035-1047
ISSN
2352-3409
Publisher
Elsevier
Start Page
1035
End Page
1047
Journal / Book Title
Data in Brief
Volume
5
Copyright Statement
© 2015 The Authors. Published by Elsevier Inc. This is an open
access article under the CC BY-NC-ND license
(http://creativecommons.org/licenses/by-nc-nd/4.0/).
access article under the CC BY-NC-ND license
(http://creativecommons.org/licenses/by-nc-nd/4.0/).
License URL
Sponsor
Engineering & Physical Science Research Council (E
Engineering & Physical Science Research Council (E
Wellcome Trust
Wellcome Trust
Grant Number
N/a
EPSRC Grant EP/G037604/1
093378/Z/10/Z
108430/Z/15/Z
Subjects
Glycan microarray
Lectin
ArtinM
Artocarpus heterophyllus
Immunomodulation
Publication Status
Published