Exploring the glycans of Euglena gracilis

O’Neill, Ellis C., Kuhaudomlarp, Sakonwan, Rejzek, Martin, Fangel, Jonatan U., Alagesan, Kathirvel, Kolarich, Daniel, Willats, William G.T. and Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275 (2017) Exploring the glycans of Euglena gracilis. Biology, 6 (4). ISSN 2079-7737

Full text not available from this repository. (Request a copy)

Abstract

Euglena gracilis is an alga of great biotechnological interest and extensive metabolic capacity, able to make high levels of bioactive compounds, such as polyunsaturated fatty acids, vitamins and β-glucan. Previous work has shown that Euglena expresses a wide range of carbohydrate-active enzymes, suggesting an unexpectedly high capacity for the synthesis of complex carbohydrates for a single-celled organism. Here, we present an analysis of some of the carbohydrates synthesised by Euglena gracilis. Analysis of the sugar nucleotide pool showed that there are the substrates necessary for synthesis of complex polysaccharides, including the unusual sugar galactofuranose. Lectin- and antibody-based profiling of whole cells and extracted carbohydrates revealed a complex galactan, xylan and aminosugar based surface. Protein N-glycan profiling, however, indicated that just simple high mannose-type glycans are present and that they are partially modified with putative aminoethylphosphonate moieties. Together, these data indicate that Euglena possesses a complex glycan surface, unrelated to plant cell walls, while its protein glycosylation is simple. Taken together, these findings suggest that Euglena gracilis may lend itself to the production of pharmaceutical glycoproteins.

Item Type: Article
Additional Information: Funding Information: Supplementary Materials: The following are available online at www.mdpi.com/2079-7737/6/4/45/s1, Table S1: Number of Euglena transcripts encoding proteins in each of the CAZyme families, Table S2: Standards of sugar nucleotides detected in the photoautotrophic culture of Euglena gracilis: relative retention times and MRM transitions, Table S3: Specificity of the antibodies used in the immunocarbohydrate microarray profiling Acknowledgments: This work was supported by the UK BBSRC Institute Strategic Programme on Understanding and Exploiting Metabolism (MET) [BB/J004561/1]; the John Innes Foundation; the Royal Thai Government Scholarship programme. Ellis C. O’Neill is supported by a Violette and Samuel Glasstone Independent Research Fellowship. D.K. acknowledges support by the European Union (Seventh Framework Programme “Glycoproteomics” project, grant number PCIG09-GA-2011-293847). We thank the Beilstein-Institut for supporting K.A. with a Ph.D. scholarship and the Max Planck Society for financial support. The authors would like to thank Lionel Hill for assistance with mass spectrometry of sugar nucleotides, and Ben Wagstaff, Ed Hems and Nick Smirnoff for sugar nucleotide standards. Funding Information: This work was supported by the UK BBSRC Institute Strategic Programme on Understanding and Exploiting Metabolism (MET) [BB/J004561/1]; the John Innes Foundation; the Royal Thai Government Scholarship programme. Ellis C. O’Neill is supported by a Violette and Samuel Glasstone Independent Research Fellowship. D.K. acknowledges support by the European Union (Seventh Framework Programme “Glycoproteomics” project, grant number PCIG09-GA-2011-293847). We thank the Beilstein-Institut for supporting K.A. with a Ph.D. scholarship and the Max Planck Society for financial support. The authors would like to thank Lionel Hill for assistance with mass spectrometry of sugar nucleotides, and Ben Wagstaff, Ed Hems and Nick Smirnoff for sugar nucleotide standards. Publisher Copyright: © 2017 by the authors. Licensee MDPI, Basel, Switzerland.
Uncontrolled Keywords: algae,biotechnology,carbohydrates,euglena,n-glycan,sugar nucleotide,biochemistry, genetics and molecular biology(all),immunology and microbiology(all),agricultural and biological sciences(all) ,/dk/atira/pure/subjectarea/asjc/1300
Faculty \ School:
Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 04 Sep 2024 09:35
Last Modified: 25 Sep 2024 18:06
URI: https://ueaeprints.uea.ac.uk/id/eprint/96508
DOI: 10.3390/biology6040045

Actions (login required)

View Item View Item