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Profiling serum antibodies with a pan allergen phage library identifies key wheat allergy epitopes

Author

Listed:
  • Daniel R. Monaco

    (Johns Hopkins School of Medicine)

  • Brandon M. Sie

    (Harvard Medical School)

  • Thomas R. Nirschl

    (Johns Hopkins School of Medicine)

  • Audrey C. Knight

    (Johns Hopkins School of Medicine)

  • Hugh A. Sampson

    (Icahn School of Medicine at Mount Sinai)

  • Anna Nowak-Wegrzyn

    (Icahn School of Medicine at Mount Sinai)

  • Robert A. Wood

    (Johns Hopkins Hospital)

  • Robert G. Hamilton

    (Johns Hopkins University School of Medicine)

  • Pamela A. Frischmeyer-Guerrerio

    (National Institutes of Allergy and Infectious Diseases)

  • H. Benjamin Larman

    (Johns Hopkins School of Medicine)

Abstract

Allergic reactions occur when IgE molecules become crosslinked by antigens such as food proteins. Here we create the ‘AllerScan’ programmable phage display system to characterize the binding specificities of anti-allergen IgG and IgE antibodies in serum against thousands of allergenic proteins from hundreds of organisms at peptide resolution. Using AllerScan, we identify robust anti-wheat IgE reactivities in wheat allergic individuals but not in wheat-sensitized individuals. Meanwhile, a key wheat epitope in alpha purothionin elicits dominant IgE responses among allergic patients, and frequent IgG responses among sensitized and non-allergic patients. A double-blind, placebo-controlled trial shows that alpha purothionin reactivity, among others, is strongly modulated by oral immunotherapy in tolerized individuals. AllerScan may thus serve as a high-throughput platform for unbiased analysis of anti-allergen antibody specificities.

Suggested Citation

  • Daniel R. Monaco & Brandon M. Sie & Thomas R. Nirschl & Audrey C. Knight & Hugh A. Sampson & Anna Nowak-Wegrzyn & Robert A. Wood & Robert G. Hamilton & Pamela A. Frischmeyer-Guerrerio & H. Benjamin La, 2021. "Profiling serum antibodies with a pan allergen phage library identifies key wheat allergy epitopes," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20622-1
    DOI: 10.1038/s41467-020-20622-1
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    Cited by:

    1. Anna-Maria Liebhoff & Thiagarajan Venkataraman & William R. Morgenlander & Miso Na & Tomasz Kula & Kathleen Waugh & Charles Morrison & Marian Rewers & Randy Longman & June Round & Stephen Elledge & In, 2024. "Efficient encoding of large antigenic spaces by epitope prioritization with Dolphyn," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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