Cabbage lipid transfer protein Bra o 3 is a major allergen responsible for cross-reactivity between plant foods and pollens

Introduction: Allergy to nonspecific lipid transfer protein (nsLTP) is the main cause of plant-food allergy in Spain. nsLTPs are widely distributed in the plant kingdom and have high cross-reactivity but extremely variable clinical expression. Little is known about the natural evolution of this allergy, which complicates management. The objective of this study was to assess the development of allergy to new plant foods in nsLTP-sensitized patients 10 years after diagnosis. Methods: One hundred fifty-one patients showing specific IgE to nsLTP determined by ISAC (Thermofisher) were included. After clinical workup (i.e., anamnesis, skin test, and challenge when needed), these patients were divided into two groups: 113 patients allergic to one or more plant food (74.5%) and 38 patients not allergic to any plant food (25.1%). Ten years later, a telephone interview was conducted to check whether patients had developed additional allergic reactions to plant foods. Results: Ten years after diagnosis, 35 of the 113 (31%) plant-food-allergic patients sensitized to nsLTP reported reactions to new, previously tolerated plant foods, mainly Rosaceae/Prunoideae fruits and nuts followed by vegetables, Rosacea/Pomoideae fruits, legumes, and cereals. Five out of 38 (13.2%) patients previously sensitized to nsLTP but without allergy to any plant food had experienced allergic reactions to some plant food: two to Rosaceae/Prunoideae fruits, two to Rosaceae/Prunoideae fruit and nuts, and one to legumes. Conclusion: Patients sensitized to nsLTP developed allergic reactions to other plant foods, mainly Rosaceae-Prunoideae fruits and nuts. This was more frequent among plant-food-allergic patients than among those who had never had plant-food allergy.

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Plant Lipid Transfer Protein Allergens: No Cross-Reactivity between Those from Foods and Olive and Parietaria Pollen

International Archives of Allergy and Immunology ◽

10.1159/000323503 ◽

2011 ◽

Vol 156 (3) ◽

pp. 291-296 ◽

Cited By ~ 37

Author(s):

Leticia Tordesillas ◽

Sofía Sirvent ◽

Araceli Díaz-Perales ◽

Mayte Villalba ◽

Javier Cuesta-Herranz ◽

...

Keyword(s):

Lipid Transfer Protein ◽

Cross Reactivity ◽

Lipid Transfer ◽

Plant Lipid ◽

Transfer Protein

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Cloning and Characterization of Walnut Lipid Transfer Protein: Not a Major Allergen in Walnut-Allergic U.S. Patients

Journal of Allergy and Clinical Immunology ◽

10.1016/j.jaci.2005.12.178 ◽

2006 ◽

Vol 117 (2) ◽

pp. S43 ◽

Cited By ~ 1

Author(s):

S.S. Teuber ◽

E. Pastorello ◽

W.R. Peterson ◽

A.M. Dandekar ◽

S. Uratsu

Keyword(s):

Lipid Transfer Protein ◽

Major Allergen ◽

Lipid Transfer ◽

Transfer Protein

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Cas S 8, the Lipid Transfer Protein from Chestnut Seeds, is a Major Allergen in Chestnut Allergic Patients without Associated Latex Allergy, but not in those with the Latex-Fruit Syndrome

Journal of Allergy and Clinical Immunology ◽

10.1016/j.jaci.2005.12.192 ◽

2006 ◽

Vol 117 (2) ◽

pp. S47 ◽

Cited By ~ 1

Author(s):

C. Blanco ◽

R. Sánchez-Monge ◽

M. Recas ◽

G. López-Torrejón ◽

J. Cumplido ◽

...

Keyword(s):

Lipid Transfer Protein ◽

Major Allergen ◽

Latex Allergy ◽

Lipid Transfer ◽

Transfer Protein ◽

Fruit Syndrome

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Evidence for a lipid transfer protein as the major allergen of apricot

Journal of Allergy and Clinical Immunology ◽

10.1016/s0091-6749(00)90090-3 ◽

2000 ◽

Vol 105 (2) ◽

pp. 371-377 ◽

Cited By ~ 60

Author(s):

Elide A. Pastorello ◽

Francesco Purello D’Ambrosio ◽

Valerio Pravettoni ◽

Laura Farioli ◽

Gabriella Giuffrida ◽

...

Keyword(s):

Lipid Transfer Protein ◽

Major Allergen ◽

Lipid Transfer ◽

Transfer Protein

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Anaphylaxis to plant-foods and pollen allergens in patients with lipid transfer protein syndrome

Current Opinion in Allergy and Clinical Immunology ◽

10.1097/aci.0b013e32835f5b07 ◽

2013 ◽

Vol 13 (4) ◽

pp. 379-385 ◽

Cited By ~ 39

Author(s):

Riccardo Asero ◽

Valerio Pravettoni

Keyword(s):

Lipid Transfer Protein ◽

Lipid Transfer ◽

Pollen Allergens ◽

Plant Foods ◽

Transfer Protein

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Sensitization Prevalence, Antibody Cross-Reactivity and Immunogenic Peptide Profile of Api g 2, the Non-Specific Lipid Transfer Protein 1 of Celery

PLoS ONE ◽

10.1371/journal.pone.0024150 ◽

2011 ◽

Vol 6 (8) ◽

pp. e24150 ◽

Cited By ~ 37

Author(s):

Gabriele Gadermaier ◽

Michael Hauser ◽

Matthias Egger ◽

Rosetta Ferrara ◽

Peter Briza ◽

...

Keyword(s):

Lipid Transfer Protein ◽

Cross Reactivity ◽

Lipid Transfer ◽

Peptide Profile ◽

Transfer Protein ◽

Immunogenic Peptide ◽

Specific Lipid

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Energy Landscapes of Ligand Motion Inside the Tunnel-Like Cavity of Lipid Transfer Proteins: The Case of the Pru p 3 Allergen

International Journal of Molecular Sciences ◽

10.3390/ijms20061432 ◽

2019 ◽

Vol 20 (6) ◽

pp. 1432

Author(s):

Bruno Cuevas-Zuviría ◽

María Garrido-Arandia ◽

Araceli Díaz-Perales ◽

Luis Pacios

Keyword(s):

Lipid Transfer Protein ◽

Protein A ◽

Major Allergen ◽

Cross Reactivity ◽

Food Sources ◽

Carrier Protein ◽

Binding Modes ◽

Lipid Transfer ◽

Collective Variables ◽

Pru P 3

Allergies are a widespread problem in western countries, affecting a large part of the population, with levels of prevalence increasingly rising due to reasons still not understood. Evidence accumulated in recent years points to an essential role played by ligands of allergen proteins in the sensitization phase of allergies. In this regard, we recently identified the natural ligand of Pru p 3, a lipid transfer protein, a major allergen from peach fruit and a model of food allergy. The ligand of Pru p 3 has been shown to play a key role in the sensitization to peach and to other plant food sources that provoke cross-reactivity in a large proportion of patients allergic to peach. However, the question of which is the binding pose of this ligand in its carrier protein, and how it can be transferred to receptors of the immune system where it develops its function as a coadjuvant was not elucidated. In this work, different molecular dynamics simulations have been considered as starting points to study the properties of the ligand–protein system in solution. Besides, an energy landscape based on collective variables that describe the process of ligand motion within the cavity of Pru p 3 was obtained by using well-tempered metadynamics. The simulations revealed the differences between distinct binding modes, and also revealed important aspects of the motion of the ligand throughout its carrier protein, relevant to its binding–unbinding process. Our findings are potentially interesting for studying protein–ligand systems beyond the specific case of the allergen protein dealt with here.

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