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Vol. 124, No. 1-3, 2001
Issue release date: January–March 2001
Section title: Allergens
Int Arch Allergy Immunol 2001;124:67–69
(DOI:10.1159/000053671)

Lipid Transfer Protein: A Pan-Allergen in Plant-Derived Foods That Is Highly Resistant to Pepsin Digestion

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.
aAmbulatorio di Allergologia, Ospedale Caduti Bollatesi, Bollate, and bLofarma SpA, Milan, Italy; cDepartment of Molecular Biology, Agricultural University of Wageningen, and dDepartment of Allergy, CLB and Laboratory for Experimental and Clinical Immunology, Academic Medical Centre, University of Amsterdam, and eDepartment of Allergology, Prinsengracht Hospital, Amsterdam, The Netherlands; fUnité de Biochimie et Biologie Moléculaire des Céréales, INRA, Montpellier, France

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Article / Publication Details

First-Page Preview
Abstract of Allergens

Published online: 1/24/2012
Issue release date: January–March 2001

Number of Print Pages: 3
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA

Abstract

Background: Lipid transfer proteins (LTPs) are stable and highly conserved proteins of around 10 kD. They have recently been identified as allergens in fruits of the Rosaceae family. Objective: The aim of this study was to investigate whether the highly conserved structure of LTPs justifies a designation as a true pan-allergen, and to study the role of protein stability in allergenicity. Methods: Thirty-eight patients with a positive skin prick test to Rosaceae fruit extracts were characterized by interviews and skin prick tests. 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 natural and recombinant LTPs. To address the role of protein stability in the allergenicity of LTP, fruit extracts and LTPs were digested with pepsin. Results: IgE antibodies to Rosaceae LTPs cross-reacted with a broad range of non-Rosaceae vegetable foods. Inhibition studies with purified natural and recombinant LTPs confirmed the role of LTP in this cross-reactivity. Many of the patients with this type of cross-reactive IgE antibodies had a clinical food allergy. In contrast to the typical birch Rosaceae cross-reactive patients, the oral allergy syndrome was frequently accompanied by more severe and systemic reactions. IgE reactivity to LTP was shown to be resistant to pepsin treatment of the allergen. Conclusion: LTP is a true 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.


  

Author Contacts

Correspondence to: Dr. R. van Ree
CLB, Department of Allergy
Plesmanlaan 125
NL–1066 CX, Amsterdam (The Netherlands)
Tel. +31 20 512 3242, Fax +31 20 512 3170, E-Mail r_van_ree@clb.nl

  

Article Information

Number of Print Pages : 3
Number of Figures : 0, Number of Tables : 0, Number of References : 20

  

Publication Details

International Archives of Allergy and Immunology
Founded 1950

Vol. 124, No. 1-3, Year 2001 (Cover Date: January-March 2001)

Journal Editor: D. Kraft, Vienna
ISSN: 1018–2438 (print), 1423–0097 (Online)

For additional information:http://www.karger.com/journals/iaa


Article / Publication Details

First-Page Preview
Abstract of Allergens

Published online: 1/24/2012
Issue release date: January–March 2001

Number of Print Pages: 3
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA


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