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Peer-reviewedCC BY 4.0International Journal of Molecular Sciences

Heterologous Expression and Immunoreactivity of Wheat Amylase–Trypsin Inhibitors

  • Lisa Call1
  • Thomas Svoboda1
  • Andrea Krisai1
  • Tim Hacker1
  • Kathrin Lauter1
  • Stefano D’Amico2
  • Birgit Linhart3
  • Agnès Amouric4
  • Mickaël Lafond4
  • Thierry Giardina4
  • Motohiro Ebisawa5
  • Rudolf Valenta3,6
1 more authors
  • Heinrich Grausgruber1
6 affiliations
  1. 1Department of Agricultural Sciences, BOKU University, 3430 Tulln an der Donau, Austria
  2. 2AGES—Austrian Agency for Health and Food Safety, 1220 Vienna, Austria
  3. 3Institute of Pathophysiology and Allergy Research, Medical University of Vienna, 1090 Vienna, Austria
  4. 4iSm2, CNRS, Aix-Marseille Université, Centrale Marseille, 13397 Marseille, France
  5. 5Clinical Research Center for Allergy and Rheumatology, NHO Sagamihara National Hospital, Sagamihara 252-0392, Kanagawa, Japan
  6. 6Center for Molecular Allergology, Karl Landsteiner University of Health Sciences, 3500 Krems, Austria
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Abstract

Wheat amylase–trypsin inhibitors (ATIs) are known for their allergenic properties, but their precise role in celiac disease and other wheat-related disorders remains unclear. Pure ATI preparations provide a basis for detailed biochemical and immunologic characterization; however, the complexity of isolating ATIs in the absence of other immunoreactive wheat proteins is an ongoing challenge. To address this limitation, bacterial and yeast heterologous expression systems were evaluated for the production of pure ATI preparations. While the synthesis of recombinant ATIs 0.28 and CM3 in Escherichia coli was challenging regarding protein solubility, promising results were observed for ATIs 0.19, CM1 and CM3 expressed in Pichia pastoris, both in terms of solubility and protein yields. The biochemical and immunoreactive properties of these recombinant ATIs were evaluated by SDS-PAGE, MALDI-TOF MS, LC-MS/MS, circular dichroism analysis, and in vitro inhibitory and immunoassays, and compared to native ATIs isolated from wheat. Our findings shed light on the difficulties in isolating pure ATIs and provide valuable insights into the potential impact of these proteins on human health. By using innovative expression systems, we aim to contribute to the detailed biochemical and immunogenic characterization of ATIs and improve the understanding of their role in wheat-related disorders and associated allergic responses.

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Cite

BibTeXRIS
BibTeX
@article{call2026heterologous,
  title = {{Heterologous Expression and Immunoreactivity of Wheat Amylase–Trypsin Inhibitors}},
  author = {Lisa Call and Thomas Svoboda and Andrea Krisai and Tim Hacker and Kathrin Lauter and Stefano D’Amico and Birgit Linhart and Agnès Amouric and Mickaël Lafond and Thierry Giardina and Motohiro Ebisawa and Rudolf Valenta and Heinrich Grausgruber},
  journal = {International Journal of Molecular Sciences},
  year = {2026},
  month = oct,
  doi = {10.3390/ijms27198857},
  url = {https://www.mdpi.com/1422-0067/27/19/8857},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Heterologous Expression and Immunoreactivity of Wheat Amylase–Trypsin Inhibitors
AU  - Lisa Call
AU  - Thomas Svoboda
AU  - Andrea Krisai
AU  - Tim Hacker
AU  - Kathrin Lauter
AU  - Stefano D’Amico
AU  - Birgit Linhart
AU  - Agnès Amouric
AU  - Mickaël Lafond
AU  - Thierry Giardina
AU  - Motohiro Ebisawa
AU  - Rudolf Valenta
AU  - Heinrich Grausgruber
PY  - 2026
DA  - 2026/10/04
JO  - International Journal of Molecular Sciences
DO  - 10.3390/ijms27198857
UR  - https://www.mdpi.com/1422-0067/27/19/8857
AB  - Wheat amylase–trypsin inhibitors (ATIs) are known for their allergenic properties, but their precise role in celiac disease and other wheat-related disorders remains unclear. Pure ATI preparations provide a basis for detailed biochemical and immunologic characterization; however, the complexity of isolating ATIs in the absence of other immunoreactive wheat proteins is an ongoing challenge. To address this limitation, bacterial and yeast heterologous expression systems were evaluated for the production of pure ATI preparations. While the synthesis of recombinant ATIs 0.28 and CM3 in Escherichia coli was challenging regarding protein solubility, promising results were observed for ATIs 0.19, CM1 and CM3 expressed in Pichia pastoris, both in terms of solubility and protein yields. The biochemical and immunoreactive properties of these recombinant ATIs were evaluated by SDS-PAGE, MALDI-TOF MS, LC-MS/MS, circular dichroism analysis, and in vitro inhibitory and immunoassays, and compared to native ATIs isolated from wheat. Our findings shed light on the difficulties in isolating pure ATIs and provide valuable insights into the potential impact of these proteins on human health. By using innovative expression systems, we aim to contribute to the detailed biochemical and immunogenic characterization of ATIs and improve the understanding of their role in wheat-related disorders and associated allergic responses.
SN  - 1422-0067
SN  - 1661-6596
ER  -