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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

Fluorescence-based solid-phase assays to study glycan-binding protein interactions with glycoconjugates.

Anne Leppänen1, Richard D Cummings

  • 1Department of Biosciences, Division of Biochemistry, University of Helsinki, Viikinkaari, Helsinki, Finland.

Methods in Enzymology
|September 7, 2010
PubMed
Summary

This study introduces a new fluorescence-based assay for studying glycan-binding protein (GBP) interactions with natural glycoconjugates like cells and glycopeptides. This versatile method enhances understanding of complex GBP binding specificities beyond traditional glycan microarrays.

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Area of Science:

  • Carbohydrate Chemistry
  • Biochemistry
  • Molecular Biology

Background:

  • Glycan microarray technologies have advanced the study of glycan-binding protein (GBP) specificities.
  • Current glycan arrays are limited to simpler structures like N-glycans and oligosaccharides, excluding complex glycoconjugates.
  • Certain GBPs, such as selectins, require peptide components for high-affinity binding, which are not typically included in standard glycan arrays.

Purpose of the Study:

  • To develop a versatile assay for studying complex GBP-glycoconjugate interactions.
  • To overcome the limitations of traditional glycan microarrays by incorporating natural glycoconjugates.
  • To investigate the binding specificities of GBPs to a wider range of biological ligands.

Main Methods:

  • A fluorescence-based solid-phase assay using commercial streptavidin-coated microplates.
  • Immobilization of various biotinylated ligands, including glycopeptides, oligosaccharides, and whole cells (mammalian and microbial).
  • Detection of GBP binding using fluorescently labeled GBPs, cells, or anti-GBP antibodies.

Main Results:

  • Demonstrated a versatile method for studying GBP interactions with immobilized natural glycoconjugates.
  • Successfully studied the binding of P-selectin, L-selectin, and galectin-1 to glycopeptides, oligosaccharides, and cells.
  • Showcased the utility of biotinylated and fixed cells for analyzing GBP adhesion.

Conclusions:

  • The developed assay provides a valuable tool for studying complex GBP-glycoconjugate interactions beyond the scope of traditional glycan microarrays.
  • This method enables the investigation of GBPs with more natural and complex ligands, including whole cells.
  • The approach facilitates a deeper understanding of GBP functions in biological systems by utilizing diverse glycoconjugate formats.