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Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion.
Int Arch Allergy Immunol 2000; 122(1):20-32IA

Abstract

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.

Authors+Show Affiliations

Ambulatorio di Allergologia, Ospedale Caduti Bollatesi, Bollate, Italy.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

10859466

Citation

Asero, R, et al. "Lipid Transfer Protein: a Pan-allergen in Plant-derived Foods That Is Highly Resistant to Pepsin Digestion." International Archives of Allergy and Immunology, vol. 122, no. 1, 2000, pp. 20-32.
Asero R, Mistrello G, Roncarolo D, et al. Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int Arch Allergy Immunol. 2000;122(1):20-32.
Asero, R., Mistrello, G., Roncarolo, D., de Vries, S. C., Gautier, M. F., Ciurana, C. L., ... 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, 122(1), pp. 20-32.
Asero R, et al. Lipid Transfer Protein: a Pan-allergen in Plant-derived Foods That Is Highly Resistant to Pepsin Digestion. Int Arch Allergy Immunol. 2000;122(1):20-32. PubMed PMID: 10859466.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. AU - Asero,R, AU - Mistrello,G, AU - Roncarolo,D, AU - de Vries,S C, AU - Gautier,M F, AU - Ciurana,C L, AU - Verbeek,E, AU - Mohammadi,T, AU - Knul-Brettlova,V, AU - Akkerdaas,J H, AU - Bulder,I, AU - Aalberse,R C, AU - van Ree,R, PY - 2000/6/22/pubmed PY - 2000/6/22/medline PY - 2000/6/22/entrez SP - 20 EP - 32 JF - International archives of allergy and immunology JO - Int. Arch. Allergy Immunol. VL - 122 IS - 1 N2 - 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. SN - 1018-2438 UR - https://www.unboundmedicine.com/medline/citation/10859466/Lipid_transfer_protein:_a_pan_allergen_in_plant_derived_foods_that_is_highly_resistant_to_pepsin_digestion_ L2 - https://www.karger.com?DOI=10.1159/000024355 DB - PRIME DP - Unbound Medicine ER -