Mapping invisible epitopes by NMR spectroscopy

Emery T. Usher, Scott A. Showalter

Research output: Contribution to journalReview articlepeer-review

Abstract

Defining discontinuous antigenic epitopes remains a substantial challenge, as exemplified by the case of lipid transfer poly-proteins, 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.

Original languageEnglish (US)
Pages (from-to)17411-17412
Number of pages2
JournalJournal of Biological Chemistry
Volume295
Issue number51
DOIs
StatePublished - Dec 18 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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