Noncovalent microarrays from synthetic amino-terminating glycans: Implications in expanding glycan microarray diversity and platform comparison

Author:

Li Chunxia12,Palma Angelina S3,Zhang Pengtao1,Zhang Yibing4,Gao Chao4,Silva Lisete M4,Li Zhen4,Trovão Filipa3,Weishaupt Markus5,Seeberger Peter H5,Likhosherstov Leonid M6,Piskarev Vladimir7,Yu Jin8,Westerlind Ulrika8,Chai Wengang4

Affiliation:

1. Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy and Shandong Provincial Key laboratory of Glycoscience and Glycoengineering, Ocean University of China, 5 Yushan Road, Qingdao 266003, China

2. Laboratory for Marine Drugs and Bioproducts, Pilot National Laboratory for Marine Science and Technology (Qingdao), Wenhai Road, Qingdao 266237, China

3. Applied Molecular Biosciences Unit, Department of Chemistry, School of Science and Technology, NOVA University of Lisbon, Campus de, 1099-085 Lisboa, Portugal

4. Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Du Cane Road, London W12 0NN, United Kingdom

5. Department of Biomolecular Systems, Max-Planck-Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam, Germany

6. N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninskiy Prospekt 47, Moscow 119334, Russia

7. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Vavilova St. 28, Moscow V-334, 119991, Russia

8. Umeå University, Department of Chemistry, KBC-building, Linneaus väg 6, S-907 36 Umeå, Sweden

Abstract

Abstract Glycan microarrays have played important roles in detection and specificity assignment of glycan recognition by proteins. However, the size and diversity of glycan libraries in current microarray systems are small compared to estimated glycomes, and these may lead to missed detection or incomplete assignment. For microarray construction, covalent and noncovalent immobilization are the two types of methods used, but a direct comparison of results from the two platforms is required. Here we develop a chemical strategy to prepare lipid-linked probes from both naturally derived aldehyde-terminating and synthetic amino-terminating glycans that addresses the two aspects: expansion of sequence-defined glycan libraries and comparison of the two platforms. We demonstrate the specific recognition by plant and mammalian lectins, carbohydrate-binding modules and antibodies and the overall similarities from the two platforms. Our results provide new knowledge on unique glycan-binding specificities for the immune receptor Dectin-1 toward β-glucans and the interaction of rotavirus P[19] adhesive protein with mucin O-glycan cores.

Funder

Wellcome Trust Biomedical Resource

National Science and Technology Major Project for Significant New Drugs Development

Portuguese Foundation for Science and Technology

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

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