IgE-Binding Capacity and Cross-Reactivity of Lipid-Transfer-Proteins (LTP) from Peach (Pru p 3) and Hazelnut (Cor a 8)

Previously, we isolated the lentil allergen Len c 3, belonging to the class of lipid transfer proteins, cross-reacting with the major peach allergen Pru p 3 and binding lipid ligands. In this work, the allergenic capacity of Len c 3 and effects of different lipid ligands on the protein stability and IgE-binding capacity were investigated. Impacts of pH and heat treating on ligand binding with Len c 3 were also studied. It was shown that the recombinant Len c 3 (rLen c 3) IgE-binding capacity is sensitive to heating and simulating of gastroduodenal digestion. While being heated or digested, the protein showed a considerably lower capacity to bind specific IgE in sera of allergic patients. The presence of lipid ligands increased the thermostability and resistance of rLen c 3 to digestion, but the level of these effects was dependent upon the ligand’s nature. The anionic lysolipid LPPG showed the most pronounced protective effect which correlated well with experimental data on ligand binding. Thus, the Len c 3 stability and allergenic capacity can be retained in the conditions of food heat cooking and gastroduodenal digestion due to the presence of certain lipid ligands.

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Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

Clinical and Developmental Immunology ◽

10.1155/2013/385615 ◽

2013 ◽

Vol 2013 ◽

pp. 1-12 ◽

Cited By ~ 6

Author(s):

C. Gómez-Casado ◽

M. Garrido-Arandia ◽

P. Gamboa ◽

N. Blanca-López ◽

G. Canto ◽

...

Keyword(s):

Food Allergy ◽

Ex Vivo ◽

Binding Capacity ◽

Cross Reactivity ◽

T Cell Epitopes ◽

Native Form ◽

Ige Binding ◽

Pru P 3

Nowadays, treatment of food allergy only considered the avoidance of the specific food. However, the possibility of cross-reactivity makes this practice not very effective. Immunotherapy may exhibit as a good alternative to food allergy treatment. The use of hypoallergenic molecules with reduced IgE binding capacity but with ability to stimulate the immune system is a promising tool which could be developed for immunotherapy. In this study, three mutants of Pru p 3, the principal allergen of peach, were produced based on the described mimotope and T cell epitopes, by changing the specific residues to alanine, named asPru p 3.01, Pru p 3.02, andPru p 3.03.Pru p 3.01showed very similar allergenic activity as the wild type byin vitroassays. However,Pru p 3.02andPru p 3.03presented reduced IgE binding with respect to the native form, byin vitro,ex vivo,and in vivo assays. In addition,Pru p 3.03had affected the IgG4 binding capacity and presented a random circular dichroism, which was reflected in the nonrecognition by specific antibodies anti-Pru p 3. Nevertheless, bothPru p 3.02andPru p 3.03maintained the binding to IgG1 and their ability to activate T lymphocytes. Thus,Pru p 3.02andPru p 3.03could be good candidates for potential immunotherapy in peach-allergic patients.

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Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2007.11.046 ◽

2008 ◽

Vol 365 (4) ◽

pp. 685-690 ◽

Cited By ~ 33

Author(s):

Jean-Philippe Borges ◽

Annick Barre ◽

Raphaël Culerrier ◽

Claude Granier ◽

Alain Didier ◽

...

Keyword(s):

Cross Reactivity ◽

Lipid Transfer ◽

Lipid Transfer Proteins ◽

Ige Binding

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Lipid-transfer proteins as potential plant panallergens: cross-reactivity among proteins of Artemisia pollen, Castanea nut and Rosaceae fruits, with different IgE-binding capacities

Clinical & Experimental Allergy ◽

10.1046/j.1365-2222.2000.00909.x ◽

2000 ◽

Vol 30 (10) ◽

pp. 1403-1410 ◽

Cited By ~ 131

Author(s):

A. DÍaz-Perales ◽

M. Lombardero ◽

R. SÁnchez-Monge ◽

F. J. GarcÍa-Selles ◽

M. Pernas ◽

...

Keyword(s):

Cross Reactivity ◽

Lipid Transfer ◽

Lipid Transfer Proteins ◽

Ige Binding ◽

Artemisia Pollen

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Non‐specific lipid‐transfer proteins: Allergen structure and function, cross‐reactivity, sensitization, and epidemiology

Clinical and Translational Allergy ◽

10.1002/clt2.12010 ◽

2021 ◽

Vol 11 (3) ◽

Author(s):

Isabel J. Skypala ◽

Ricardo Asero ◽

Domingo Barber ◽

Lorenzo Cecchi ◽

Arazeli Diaz Perales ◽

...

Keyword(s):

Cross Reactivity ◽

Structure And Function ◽

Lipid Transfer ◽

Lipid Transfer Proteins ◽

Allergen Structure ◽

And Function ◽

Specific Lipid

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In vitro gastrointestinal digestion of the major peach allergen Pru p 3, a lipid transfer protein: Molecular characterization of the products and assessment of their IgE binding abilities

Molecular Nutrition & Food Research ◽

10.1002/mnfr.200900552 ◽

2010 ◽

Vol 54 (10) ◽

pp. 1452-1457 ◽

Cited By ~ 27

Author(s):

Valeria Cavatorta ◽

Stefano Sforza ◽

Giancarlo Aquino ◽

Gianni Galaverna ◽

Arnaldo Dossena ◽

...

Keyword(s):

Molecular Characterization ◽

Lipid Transfer Protein ◽

Lipid Transfer ◽

Gastrointestinal Digestion ◽

Transfer Protein ◽

Ige Binding ◽

In Vitro Gastrointestinal Digestion ◽

Pru P 3

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Hen’s egg allergy: an update

Bulletin of Siberian Medicine ◽

10.20538/1682-0363-2018-2-156-166 ◽

2018 ◽

Vol 17 (2) ◽

pp. 156-166

Author(s):

M. M. Fedotova ◽

O. S. Fedorova ◽

U. V. Konovalova ◽

E. M. Kamaltynova ◽

T. A. Nagaeva ◽

...

Keyword(s):

Clinical Presentation ◽

Binding Capacity ◽

Clinical Manifestations ◽

Cross Reactivity ◽

Current Data ◽

Egg Allergy ◽

Ige Binding ◽

Hen’S Egg ◽

Allergenic Proteins ◽

Common Problems

Hen’s egg allergy is one of the most common problems in pediatrics. This pathology is associated with severe clinical manifestations, often with a risk of anaphylactic reactions. This review presents current data on the epidemiology and clinical presentation, as well as aspects of the natural history and management of hen’s egg allergy. The paper will provide data on allergenic proteins of hen’s egg, including data on structure, physicochemical properties, IgE-binding capacity, and cross-reactivity. Finally, practical information about egg allergy and immunization will be presented.

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