Comparison of IgE-Binding Capacity, Cross-Reactivity and Biological Potency of Allergenic Non-Specific Lipid Transfer Proteins from Peach, Cherry and Hazelnut

2010 ◽  
Vol 153 (4) ◽  
pp. 335-346 ◽  
Author(s):  
Christina Hartz ◽  
Iris Lauer ◽  
Maria del Mar San Miguel Moncin ◽  
Anna Cistero-Bahima ◽  
Kay Foetisch ◽  
...  
Keyword(s):  
Binding Capacity ◽  
Cross Reactivity ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Ige Binding ◽  
Biological Potency ◽  
Specific Lipid

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

2006 ◽  
Vol 117 (2) ◽  
pp. S303
Author(s):  
C. Hartz ◽  
I. Lauer ◽  
J. Lidholm ◽  
K. Fötisch ◽  
M. San Miguel-Moncin ◽  
...  
Keyword(s):  
Binding Capacity ◽  
Cross Reactivity ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Ige Binding ◽  
Pru P 3

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

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

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

2008 ◽  
Vol 365 (4) ◽  
pp. 685-690 ◽  
Author(s):  
Jean-Philippe Borges ◽  
Annick Barre ◽  
Raphaël Culerrier ◽  
Claude Granier ◽  
Alain Didier ◽  
...  
Keyword(s):  
Cross Reactivity ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Ige Binding

Cross-reactivity among non-specific lipid-transfer proteins from food and pollen allergenic sources

2014 ◽  
Vol 165 ◽  
pp. 397-402 ◽  
Author(s):  
María Morales ◽  
M. Ángeles López-Matas ◽  
Raquel Moya ◽  
Jerónimo Carnés
Keyword(s):  
Cross Reactivity ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Specific Lipid

scholarly journals Impact of Different Lipid Ligands on the Stability and IgE-Binding Capacity of the Lentil Allergen Len c 3

Biomolecules ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 1668
Author(s):  
Ekaterina I. Finkina ◽  
Daria N. Melnikova ◽  
Ivan V. Bogdanov ◽  
Natalia S. Matveevskaya ◽  
Anastasia A. Ignatova ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Capacity ◽  
Heat Treating ◽  
Specific Ige ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Ige Binding ◽  
The Stability ◽  
Lower Capacity ◽  
Pru P 3

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.

scholarly journals Molecular basis of allergen cross-reactivity: Non-specific lipid transfer proteins from wheat flour and peach fruit as models

2009 ◽  
Vol 47 (2-3) ◽  
pp. 534-540 ◽  
Author(s):  
Leticia Tordesillas ◽  
Luis F. Pacios ◽  
Arancha Palacin ◽  
Santiago Quirce ◽  
Alicia Armentia ◽  
...  
Keyword(s):  
Wheat Flour ◽  
Molecular Basis ◽  
Cross Reactivity ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Peach Fruit ◽  
Specific Lipid

Clinical importance of non-specific lipid transfer proteins as food allergens

2002 ◽  
Vol 30 (6) ◽  
pp. 910-913 ◽  
Author(s):  
R. van Ree
Keyword(s):  
Clinical Importance ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Plant Food ◽  
Food Allergens ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
The Difference ◽  
Processing Stability ◽  
Specific Lipid

Non-specific lipid transfer proteins (nsLTPs) have recently been identified as plant food allergens. They are good examples of true food allergens, in the sense that they are capable of sensitizing, i.e. inducing specific IgE, as well as of eliciting severe symptoms. This is in contrast with most plant food allergens, which are recognized because of primary sensitization to related inhalant allergens (cross-reactivity), i.e. pollen allergens. The basis of the difference between the latter category and strong food allergens such as nsLTPs appears to lie in the sensitivity of the allergens to proteolytic attack and food processing. Stability allows the allergen to reach the gastrointestinal immune system in an immunogenic and allergenic conformation, allowing sensitization and induction of systemic symptoms. Stability also explains the presence of such allergens in processed foods. Together, these characteristics make nsLTPs clinically highly relevant plant food allergens and ideal tools with which to study the mechanisms involved in food allergy.

scholarly journals Unifying the two different classes of plant non-specific lipid-transfer proteins allergens classified in the WHO/IUIS allergen database through a motif with conserved sequence, structural and electrostatic features

2016 ◽  
Author(s):  
Sandeep Chakraborty
Keyword(s):  
Cross Reactivity ◽  
Full Length ◽  
Structural Motif ◽  
Lipid Transfer ◽  
Biotic And Abiotic Stress ◽  
Lipid Transfer Proteins ◽  
Conserved Sequence ◽  
A Genome ◽  
Specific Lipid

The ubiquitously occuring non-specific lipid-transfer proteins (nsLTPs) in plants are implicated in key processes like biotic and abiotic stress, seed development and lipid transport. Additionally, they constitute a panallergen multigene family present in both food and pollen. Presently there are 49 nsLTP entries in the WHO/IUIS allergen database (http://allergen.org/). Analysis of full-length allergens identified only two major classes (nsLTP1,n=32 and nsLTP2,n=2), although nsLTPs are classified into many other groups. nsLTP1 and nsLTP2 are differentiated by their sequences, molecular weights, pattern of the conserved disulphide bonds and volume of the hydrophobic cavity. The conserved R44 is present in all full length nsLTP1 allergens (only Par j 2 from Parietaria judaica has K44), while D43 is present in all but Par j 1/2 from P. judaica (residue numbering based on PDBid:2ALGA). Although, the importance of these residues is well-established in nsLTP1, the corresponding residues in nsLTP2 remain unknown. A structural motif comprising of two cysteines with a disulphide bond (C3-C50), R44 and D43 identified a congruent motif (C3/C35/R47/D42) in a nsLTP2 protein from rice (PDBid:1L6HA), using the CLASP methodology. This also provides a quantitative method to assess the cross-reactivity potential of different proteins through congruence of an epitope and its neighbouring residues. Future work will involve obtaining the PDB structure of an nsLTP2 allergen and Par j 1/2 nsLTP1 sequences with a missing D43, determine whether nsLTP from other groups beside nsLTP1/2 are allergens, and determine nsLTP allergens from other plants commonly responsible for causing allergic reactions (chickpea, walnut, etc.) based on a genome wide identification of genes with conserved allergen features and their in vitro characterization.

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