Stable Plant Food Allergens I: Lipid-Transfer Proteins
Lipid-transfer proteins (LTPs) exist in all branches of the plant kingdom (panallergens) and are able to induce both IgE sensitization and allergic reactions of different severities, including anaphylaxis. The allergens have a molecular weight of 6–10 kDa
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Stable Plant Food Allergens I: Lipid-Transfer Proteins A. Petersen, J. Kleine-Tebbe, and S. Scheurer
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Introduction
Nonspecific lipid-transfer proteins (nsLTPs, short term LTPs) exist ubiquitously in various tissues of both mono- and dicotyledonous plants and have functions both in the cytoplasmic transport of lipids and the creation of the plant cuticle (a waxy protective film covering the epidermis of leaves). Besides their role in lipophilic binding and transport, LTPs are involved in plant defense (for review see Kader 1996) and have been assigned to the class of plant stress proteins as PR-14 proteins (PR, pathogenesis-related) (van Loon and van Stein 1999).
This article is based on a publication of the authors published in 2011 in the Allergo Journal (Petersen A, Kleine-Tebbe J, Scheurer S (2011): Stabile pflanzliche Nahrungsmittelallergene – Lipid-Transfer-Proteine. Allergo J 20: 384–386) which has now been updated, extended, and translated as a book chapter. The authors gratefully thank Dr. Stefan Schülke, PhD, Paul-Ehrlich-Institute, Research Group Molecular Allergology, Langen, Germany, for his initial English translation and Dr. Steve Love, PhD, Laguna Niguel, CA, USA, for reading the manuscript, his helpful suggestions, and his final editorial assistance. A. Petersen, PhD (*) Research Center Borstel, Borstel, Germany e-mail: [email protected] J. Kleine-Tebbe, MD, Prof. Allergy & Asthma Center Westend, Outpatient Clinic Hanf, Ackermann & Kleine-Tebbe, Berlin, Germany e-mail: [email protected] S. Scheurer, PhD, Assoc Prof. Paul-Ehrlich-Institut, Federal Institute for Vaccines and Biomedicines, Langen, Germany e-mail: [email protected] © Springer International Publishing Switzerland 2017 J. Kleine-Tebbe, T. Jakob (eds.), Molecular Allergy Diagnostics, DOI 10.1007/978-3-319-42499-6_4
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LTPs are characterized by a strongly conserved, three-dimensional (3D) protein structure. Along with the structurally closely related 2S albumins and α-amylase/ protease inhibitors, LTPs belong to the prolamin protein superfamily (Radauer et al. 2008), which includes alcohol-soluble and glutamine-rich storage proteins. LTPs were first described as food allergens in 1992 in Spanish patients with a stone fruit-peach allergy. As an IgE-reactive protein (original designation Pru p 1) with a molecular mass of 8–10 kDa, it was found to be predominantly expressed in peach skin (Lleonart et al. 1992). An IgE cross-reactivity of this low molecular weight allergen in patients with food allergies was first demonstrated using extracts from stone fruit (Pastorello et al. 1994). In 1999 peach and apple LTPs were first described on a molecular level as allergenic LTPs (Pastorello et al. 1999) and designated as Pru p 3 and Mal d 3, respectively (Sánchez-Monge et al. 1999). To date (November 2016) 41 plant LTPs have been accepted as allergens by the IUIS (International Union of Immunological Sciences) Allergen Nomenclature Subcommittee. Furthermore, other LTPs with allergenic pro
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