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Lipid Transfer Protein: A Pan-Allergen in Plant-Derived Foods That Is Highly Resistant to Pepsin Digestion
Open accessAbstract
Background: Lipid transfer proteins (LTPs) are small molecules of approximately 10 kD that demonstrate high stability. They have recently been identified as allergens in the Rosaceae subfamilies of the Prunoideae (peach, apricot, plum) and of the Pomoideae (apple). They belong to a family of structurally highly conserved proteins that are also present in non-Rosaceae vegetable foods. Objective: The aim of this study was to investigate the cross-reactivity to non-Rosaceae LTPs, and to study the role of protein stability in allergenicity. Methods: Thirty-eight patients with a positive SPT to Rosaceae fruit extracts enriched for LTP were characterized by interview and SPT. To investigate IgE cross-reactivity between Rosaceae and non-Rosaceae LTPs, RAST and RAST inhibition as well as ELISA and ELISA inhibition were performed, using whole food extracts and purified LTPs. Both purified natural LTPs (peach, carrot and broccoli) and Pichia pastoris recombinant LTPs (carrot and wheat) were included. Pepsin digestion was used to address the role of stability in the allergenicity of LTPs. Results: IgE antibodies to Rosaceae LTPs reacted to a broad range of vegetable foods, including Gramineae (cereals), Leguminosae (peanut), Juglandaceae (walnut), Anacardiaceae (pistachio), Brassicaceae (broccoli), Umbelliferae (carrot, celery), Solanaceae (tomato), Cucurbitaceae (melon), and Actinidiaceae (kiwi). Binding and inhibition studies with purified natural and recombinant LTPs confirmed their role in this cross-reactivity. Many of these cross-reactivities were accompanied by clinical food allergy, frequently including systemic reactions. Antibody binding to LTP was shown to be resistant to pepsin treatment of whole extract or purified LTP. Conclusion: LTP is a pan-allergen with a degree of cross-reactivity comparable to profilin. Due to its extreme resistance to pepsin digestion, LTP is a potentially severe food allergen.
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Cites
Common epitopes of birch pollen and apples—Studies by western and northern blot
Ebner, C., Birkner, T., Valenta, R., Rumpold, H., Breitenbach, M., Scheiner, O., & Kraft, D. (1991) · Journal of Allergy and Clinical Immunology · doi:10.1016/0091-6749(91)90152-e · Cited by 278
Cited by
EAACI Molecular Allergology User's Guide
Matricardi, P. M., Kleine‐Tebbe, J., Hoffmann, H. J., Valenta, R., Hilger, C., Hofmaier, S., Aalberse, R. C., Agache, I., Asero, R., Ballmer‐Weber, B., et al. (2016) · Pediatric Allergy and Immunology · doi:10.1111/pai.12563 · Cited by 932
Self-citationMolecular properties of food allergens
Breiteneder, H., & Mills, E. N. C. (2005) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.10.022 · Cited by 359
Blein, J.-P., Coutos-Thévenot, P., Marion, D., & Ponchet, M. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(02)02284-7 · Cited by 310
Pollen-Food Allergy Syndrome in Children
Jeon, Y. H. (2020) · Clinical and Experimental Pediatrics · doi:10.3345/cep.2019.00780 · Cited by 31
Can Patients with Oral Allergy Syndrome Be at Risk of Anaphylaxis?
Skypala, I. J. (2020) · Current Opinion in Allergy & Clinical Immunology · doi:10.1097/aci.0000000000000679 · Cited by 30
Metadata
- Authors
- Asero, R., Mistrello, G., Roncarolo, D., de Vries, S. C., Gautier, M.-F., Ciurana, C. L. F., Verbeek, E., Mohammadi, T., Knul-Brettlova, V., Akkerdaas, J. H., Bulder, I., Aalberse, R. C., & van Ree, R.
- Venue
- International Archives of Allergy and Immunology
- Publisher
- S. Karger AG
- Published
- 2000
- Volume
- 122
- Issue
- 1
- Pages
- 20-32
- ISSN
- 1018-2438 (ISSN-L)
- 1423-0097
- OpenAlex
- W1972717477
- Cited by
- 365
- References
- 1
- FWCI
- 10.35
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Asero, R., Mistrello, G., Roncarolo, D., de Vries, S. C., Gautier, M.-F., Ciurana, C. L. F., Verbeek, E., Mohammadi, T., Knul-Brettlova, V., Akkerdaas, J. H., Bulder, I., Aalberse, R. C., & van Ree, R. (2000). Lipid Transfer Protein: A Pan-Allergen in Plant-Derived Foods That Is Highly Resistant to Pepsin Digestion. International Archives of Allergy and Immunology. https://doi.org/10.1159/000024355
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
