Localizing Carbohydrate Binding Sites in Proteins Using Hydrogen/Deuterium Exchange Mass Spectrometry

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• 作者：Jingjing Zhang ; Elena N. Kitova ; Jun Li…
• 关键词：Protein–carbohydrate complexes ; Hydrogen/deuterium exchange mass spectrometry ; Hydrogen bonds
• 刊名：Journal of The American Society for Mass Spectrometry
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：27
• 期：1
• 页码：83-90
• 全文大小：1,202 KB
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• 作者单位：Jingjing Zhang (1) (3)
  Elena N. Kitova (1) (3)
  Jun Li (1) (3)
  Luiz Eugenio (2) (3)
  Kenneth Ng (2) (3)
  John S. Klassen (1) (3)
  
  1. Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada
  3. Alberta Glycomics Centre, Edmonton, Alberta, Canada
  2. Department of Biological Sciences, University of Calgary, Calgary, Alberta, T2N 1N4, Canada
  
• 刊物主题：Analytical Chemistry; Biotechnology; Organic Chemistry; Proteomics; Bioinformatics;
• 出版者：Springer US
• ISSN：1879-1123

文摘

The application of hydrogen/deuterium exchange mass spectrometry (HDX-MS) to localize ligand binding sites in carbohydrate-binding proteins is described. Proteins from three bacterial toxins, the B subunit homopentamers of Cholera toxin and Shiga toxin type 1 and a fragment of Clostridium difficile toxin A, and their interactions with native carbohydrate receptors, GM₁ pentasaccharides (β-Gal-(1→3)-β-GalNAc-(1→4)[α-Neu5Ac-(2→3)]-β-Gal-(1→4)-Glc), Pk trisaccharide (α-Gal-(1→4)-β-Gal-(1→4)-Glc) and CD-grease (α-Gal-(1→3)-β-Gal-(1→4)-β-GlcNAcO(CH₂)₈CO₂CH₃), respectively, served as model systems for this study. Comparison of the differences in deuterium uptake for peptic peptides produced in the absence and presence of ligand revealed regions of the proteins that are protected against deuterium exchange upon ligand binding. Notably, protected regions generally coincide with the carbohydrate binding sites identified by X-ray crystallography. However, ligand binding can also result in increased deuterium exchange in other parts of the protein, presumably through allosteric effects. Overall, the results of this study suggest that HDX-MS can serve as a useful tool for localizing the ligand binding sites in carbohydrate-binding proteins. However, a detailed interpretation of the changes in deuterium exchange upon ligand binding can be challenging because of the presence of ligand-induced changes in protein structure and dynamics.