Microarray analyses of closely related glycoforms reveal different accessibilities of glycan determinants on N-glycan branches

Lei Li, Wanyi Guan, Gaolan Zhang, Zhigang Wu, Hai Yu, Xi Chen, Peng G. Wang

Research output: Contribution to journalArticle

Abstract

Glycans mediate a wide variety of biological roles via recognition by glycan-binding proteins (GBPs). Comprehensive knowledge of such interaction is thus fundamental to glycobiology. While the primary binding feature of GBPs can be easily uncovered by using a simple glycan microarray harboring limited numbers of glycan motifs, their fine specificities are harder to interpret. In this study, we prepared 98 closely related N-glycoforms that contain 5 common glycan epitopes which allowed the determination of the fine binding specificities of several plant lectins and anti-glycan antibodies. These N-glycoforms differ from each other at the monosaccharide level and were presented in an identical format to ensure comparability. With the analysis platform we used, it was found that most tested GBPs have preferences toward only one branch of the complex N-glycans, and their binding toward the epitope-presenting branch can be significantly affected by structures on the other branch. Fine specificities described here are valuable for a comprehensive understanding and applications of GBPs.

Original languageEnglish (US)
Pages (from-to)334-345
Number of pages12
JournalGlycobiology
Volume30
Issue number5
DOIs
StatePublished - Apr 20 2020

Keywords

  • N-glycan
  • chemoenzymatic synthesis
  • glycan-binding protein
  • glycoform
  • microarray

ASJC Scopus subject areas

  • Biochemistry

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