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Mapping invisible epitopes by NMR spectroscopy

Authors
  • Usher, Emery T.1
  • Showalter, Scott A.1, 2
  • 1 Department of Biochemistry and Molecular Biology and Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, Pennsylvania, USA
  • 2 Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania, USA
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry and Molecular Biology
Publication Date
Dec 18, 2020
Volume
295
Issue
51
Pages
17411–17412
Identifiers
DOI: 10.1074/jbc.H120.016607
PMID: 33453987
PMCID: PMC7762964
Source
PubMed Central
License
Unknown

Abstract

Defining discontinuous antigenic epitopes remains a substantial challenge, as exemplified by the case of lipid transfer polyproteins, which are common pollen allergens. Hydrogen/deuterium exchange monitored by NMR can be used to map epitopes onto folded protein surfaces, but only if the complex rapidly dissociates. Modifying the standard NMR-exchange measurement to detect substoichiometric complexes overcomes this time scale limitation and provides new insights into recognition of lipid transfer polyprotein by antibodies. In the future, this new and exciting development should see broad application to a range of tight macromolecular interactions.

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