Exploring the interactions between bacteriophage-encoded glycan binding proteins and carbohydrates

Curr Opin Struct Biol. 2015 Oct:34:69-77. doi: 10.1016/j.sbi.2015.07.006. Epub 2015 Aug 11.

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.

Publication types

  • Review

MeSH terms

  • Bacteriophages / genetics
  • Bacteriophages / metabolism*
  • Carbohydrate Metabolism*
  • Carbohydrates / chemistry
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Models, Molecular
  • Molecular Conformation
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Binding
  • Protein Engineering
  • Structure-Activity Relationship
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*
  • Viral Tropism

Substances

  • Carbohydrates
  • Carrier Proteins
  • Polysaccharides
  • Viral Proteins