Plant non-specific lipid transfer proteins: An interface between plant defence and human allergy

Salcedo, Gabriel; Sánchez‐Monge, Rosa; Barber, Domingo; Díaz‐Perales, Araceli

doi:10.1016/j.bbalip.2007.01.001

Cited by 186 publications

(228 citation statements)

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“…The major peach allergen, named Pru p 3, belongs to the lipid transfer protein (LTP) panallergen family (Sanchez-Monge et al, 1999;Pastorello et al, 1999). This protein family is widely distributed throughout the plant kingdom and includes small basic polypeptides (9 kDa; p/~ 9) with 8 conserved cysteine residues forming 4 disulphide bridges (Salcedo et al, 2004;Salcedo et al, 2007). LTPs are important allergens not only in Rosaceae fruits, but also in other plant foods, such as vegetables, cereals and nuts (Salcedo et al, 2004;Salcedo et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…This protein family is widely distributed throughout the plant kingdom and includes small basic polypeptides (9 kDa; p/~ 9) with 8 conserved cysteine residues forming 4 disulphide bridges (Salcedo et al, 2004;Salcedo et al, 2007). LTPs are important allergens not only in Rosaceae fruits, but also in other plant foods, such as vegetables, cereals and nuts (Salcedo et al, 2004;Salcedo et al, 2007). Furthermore, LTPs have also been involved in some pollinosis and in cross-reactivity between plant foods and pollens (Salcedo et al, 2007;Zuidmeer and van Ree, 2007), as well as in occupational asthma (baker's asthma) (Palacin et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…LTPs are important allergens not only in Rosaceae fruits, but also in other plant foods, such as vegetables, cereals and nuts (Salcedo et al, 2004;Salcedo et al, 2007). Furthermore, LTPs have also been involved in some pollinosis and in cross-reactivity between plant foods and pollens (Salcedo et al, 2007;Zuidmeer and van Ree, 2007), as well as in occupational asthma (baker's asthma) (Palacin et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: Peach Pru p 3 allergen as a model☆

Pacios¹,

Tordesillas²,

Cuesta‐Herranz

et al. 2008

Molecular Immunology

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Lipid transfer proteins (LTPs) are the major allergens of Rosaceae fruits in the Mediterranean area. Pru p 3, the LTP and major allergen of peach, is a suitable model for studying food allergy and amino acid sequences related with its IgE-binding capacity. In this work, we sought to map IgE mimotopes on the structure of Pru p 3, using the combination of a random peptide phage display library and a three-dimensional modelling approach. Pru p 3-specific IgE was purified from 2 different pools of sera from peach allergic patients grouped by symptoms (OAS-pool or SYS-pool), and used for screening of a random dodecapeptide phage display library. Positive clones were further confirmed by ELISA assays testing individual sera from each pool. Three-dimensional modelling allowed location of mimotopes based on analysis of electrostatic properties and solvent exposure of the Pru p 3 surface. Twenty-one phage clones were selected using Pru p 3-specific IgE, 9 of which were chosen using OAS-specific IgE while the other 12 were selected with systemic-specific IgE. Peptide alignments revealed consensus sequences for each pool: L37 R39 T40 P42 D43 R44 A46 P70 S76 P78 Y79 for OAS-IgE, and N35 N36 L37 R39 T40 D43 A46 S76177 P78 for systemic-IgE. These 2 consensus sequences were mapped on the same surface of Pru p 3, corresponding to the helix 2-loop-helix 3 region and part of the non-structured C-terminal coil. Thus, 2 relevant conformational IgE-binding regions of Pru p 3 were identified using a random peptide phage display library. Mimotopes can be used to study the interaction between allergens and IgE, and to accelerate the process to design new vaccines and new immunotherapy strategies.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: Peach Pru p 3 allergen as a model☆

Pacios¹,

Tordesillas²,

Cuesta‐Herranz

et al. 2008

Molecular Immunology

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show abstract

“…Accordingly, Pru p 3, its major allergen and lipid stress (Salcedo et al, 2007). Allergenic LTPs are highly resistant to protease digestion and heat treatments.…”

Section: Introductionmentioning

confidence: 99%

“…They are usually associated to severe and systemic clinical symptoms and can be primary sensitizers by ingestion. They are also the main allergens of several fruits, vegetables and nuts in the Mediterranean area (Salcedo et al, 2007). Altogether, these characteristics have led to propose LTPs, particularly Pru p 3, as a model of true food allergens (van Ree, 2002;Salcedo et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

T-cell epitopes of the major peach allergen, Pru p 3: Identification and differential T-cell response of peach-allergic and non-allergic subjects

Tordesillas¹,

Cuesta‐Herranz

González‐Muñoz

et al. 2009

Molecular Immunology

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Keywords:Lipid transfer protein T-cell epitope Peptide immunotherapy Plant food allergy Peach Pru p3Lipid transfer proteins (LTPs), particularly peach Pru p 3, are the most relevant plant food allergens in the South of Europe, and, therefore, their allergic properties have been extensively studied. However, neither T-cell epitopes nor their effect on the patients' T-cell response has been investigated in any member of the LTP panallergen family. The objective of the present study was to map the major T-cell epitopes of Pru p 3, as well as to evaluate their induced T-cell response in peach-allergic versus control subjects. Thus, peripheral blood mononuclear cells (PBMCs) from 18 peach-allergic patients and Pru p 3-specific T-cell lines (TCLs) from 9 of them were cultured with Pru p 3 and with a panel of 17 derived peptides (10-mer overlapping in 5 amino acids representing the full sequence of Pru p 3). Proliferation in 5-day assays was carried out via tritiated-thymidine incorporation, while IL4 and IFN7 production was assessed via sandwich enzymelinked immunosorbent tests (ELISA) of TCL culture supernatants. The results were compared to those obtained from 10 non-peach allergic control volunteers. Two consecutive peptides showed the highest activation capacity. About 74% of PBMCs and TCLs recognized them, forming a single T-epitope: Pru p 365-80-Additionally, other specific T-cell epitopes were observed. Pru p 3 2 s-35 was detected by more than 60% of TCLs from peach-allergic patients, and Pru p 345-55 only activated PBMCs from control subjects. Interestingly, TCLs from patients were associated with a Th2-type, whereas control TCLs presented a Thltype cytokine response. The major immunogenic T-cell epitope identified in Pru p 3, Pru p 365-so, is a good candidate to develop new vaccines for hypersensitivity reactions associated with LTP allergens from Rosaceae fruits.

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Food Allergens—Molecular and Immunological Characteristics

Breiteneder¹,

Mills²

2013

Food Allergy

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Plant non-specific lipid transfer proteins: An interface between plant defence and human allergy

Cited by 186 publications

References 146 publications

Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: Peach Pru p 3 allergen as a model☆

Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: Peach Pru p 3 allergen as a model☆

T-cell epitopes of the major peach allergen, Pru p 3: Identification and differential T-cell response of peach-allergic and non-allergic subjects

Food Allergens—Molecular and Immunological Characteristics

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