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], [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.

Highlights

  • Data accessibilityGraphs and table The data were generated from a NGL-based microarray system [4]

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

  • 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]

Read more

Summary

Data accessibility

Graphs and table The data were generated from a NGL-based microarray system [4]. N-ArtinM and y-ArtinM forms were biotinylated and analyzed for binding using a NGL-based microarray (in-house designation ‘Array Sets 18–22bis’) containing 255 lipid-linked glycan probes (Table 1). The data derived from the NGL-based microarray analyses provide important information on the carbohydrate binding specificities of y-ArtinM and n-ArtinM, and serve as the basis for further studies on the fine specificities of the lectins using other microarray systems or complementary techniques. We analyzed the native form of ArtinM and its yeast-derived counterpart, in terms of their ability to bind to 255 glycans distributed in a microarray platform, in order to identify whether n-ArtinM and y-ArtinM shared sugar-recognition specificity. Y-ArtinM showed higher fluorescence intensity than n-ArtinM

Materials and methods and data
Glycan microarray analyses
Funding sources
Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.