Exploring the interactions between bacteriophage-encoded glycan binding proteins and carbohydrates
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Updated: Apr 5, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
David J Simpson1, Jessica C Sacher1, Christine M Szymanski1
1Alberta Glycomics Centre and Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada T6G 2E9.
Abstract:
There is an unprecedented interest in glycobiology due to the increasing appreciation of its impact on all aspects of life. Likewise, bacteriophage biology is enjoying a new renaissance as the post-antibiotic era fuels the search for novel ways to control harmful bacteria. Phages have spent the last 3 billion years developing ways of recognizing and manipulating bacterial surface glycans. Therefore, phages comprise a massive reservoir of glycan-binding and -hydrolyzing proteins with the potential to be exploited for glycan analysis, bacterial diagnostics and therapeutics. We discuss phage tail proteins that recognize bacterial surface polysaccharides, endolysins that bind and cleave peptidoglycan, Ig-like proteins that attach to mucin glycans, and phage effector proteins that recognize both bacterial and eukaryotic oligosaccharides.
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