Abstract

ABSTRACTThe recent article “Lectin-Glycan Interaction Network-Based Identification of Host Receptors of Microbial Pathogenic Adhesins” by Ielasi et al. describes a new development in microbial carbohydrate analysis [Ielasi FS, Alioscha-Perez M, Donohue D, Claes S, Sahli H, Schols D, Willaert RG, mBio 7(4):e00584-16, 2016, http://dx.doi.org/10.1128/mbio.00584-16]. Specific carbohydrate ligands have been identified from the patterns of lectin binding to oligosaccharides printed on a chip. The new technique links the output to a comprehensive glycan database and offers a number of data visualization options. The graphs highlight the occurrence of potential ligands, organized by organism, tissue, and patterns of association with disease states. The analysis has successfully predicted novel glycoprotein ligands for microbial lectins, including an interaction of E. coli FimH with HIV gp120.

Highlights

  • Lectins are nonenzyme proteins that bind to specific glycan determinants

  • The authors have used these data to create weighted graphs with nodes displaying the occurrence of a ligand in specific glycoproteins of organisms and their tissues, connections to other potential ligands and lectins, and association with disease states (Fig. 1D)

  • Ielasi et al confirmed these predictions by demonstrating binding to specific glycoprotein targets and by showing inhibition of binding by monosaccharide competitors [10]

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Summary

Introduction

Lectins are nonenzyme proteins that bind to specific glycan determinants. Lectins displayed on cell surfaces act as cell adhesion proteins. Several groups have reported glycochip analyses of binding specificity for several microbial lectins, including FimH from Escherichia coli, Als1 and Als3 from Candida albicans, and Epa galectins from Candida glabrata [6,7,8,9]. They have developed software that uses the glycochip results to query UniCarbKB, a comprehensive database of lectins and their ligand glycans (Fig. 1C).

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