Cross-Reactivity of IgE Antibodies with Allergens in Birch Pollen, Fruits and Vegetables

1984 ◽  
Vol 74 (3) ◽  
pp. 235-240 ◽  
Author(s):  
Liisa Halmepuro ◽  
Kaija Vuontela ◽  
Kirsti Kalimo ◽  
Fred Björkstén
Keyword(s):  
Fruits And Vegetables ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Ige Antibodies

scholarly journals Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins

2009 ◽  
Vol 29 (3) ◽  
pp. 183-192 ◽  
Author(s):  
Hanna Berkner ◽  
Philipp Neudecker ◽  
Diana Mittag ◽  
Barbara K. Ballmer-Weber ◽  
Kristian Schweimer ◽  
...  
Keyword(s):  
Physiological Function ◽  
Three Dimensional ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Food Allergens ◽  
Homologous Proteins ◽  
Allergen Specific Immunotherapy ◽  
Ige Antibodies ◽  
Bet V 1 ◽  
Yellow Lupine

In many cases, patients allergic to birch pollen also show allergic reactions after ingestion of certain fruits or vegetables. This observation is explained at the molecular level by cross-reactivity of IgE antibodies induced by sensitization to the major birch pollen allergen Bet v 1 with homologous food allergens. As IgE antibodies recognize conformational epitopes, a precise structural characterization of the allergens involved is necessary to understand cross-reactivity and thus to develop new methods of allergen-specific immunotherapy for allergic patients. Here, we report the three-dimensional solution structure of the soybean allergen Gly m 4, a member of the superfamily of Bet v 1 homologous proteins and a cross-reactant with IgE antibodies originally raised against Bet v 1 as shown by immunoblot inhibition and histamine release assays. Although the overall fold of Gly m 4 is very similar to that of Bet v 1, the three-dimensional structures of these proteins differ in detail. The Gly m 4 local structures that display those differences are also found in proteins from yellow lupine with known physiological function. The three-dimensional structure of Gly m 4 may thus shed some light on the physiological function of this subgroup of PR10 proteins (class 10 of pathogenesis-related proteins) and, in combination with immunological data, allow us to propose surface patches that might represent cross-reactive epitopes.

Cross-reactivity among birch pollen, vegetables and fruits as detected by IgE antibodies is due to at least three distinct cross-reactive structures

Allergy ◽  
1987 ◽  
Vol 42 (5) ◽  
pp. 382-390 ◽  
Author(s):  
P. G. Calkhoven ◽  
M. Aalbers ◽  
V. L. Koshte ◽  
O. Pos ◽  
H. D. Oei ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Cross Reactivity ◽  
Ige Antibodies ◽  
Vegetables And Fruits

scholarly journals Peanut-specific IgE antibodies in asymptomatic Ghanaian children possibly caused by carbohydrate determinant cross-reactivity

2013 ◽  
Vol 132 (3) ◽  
pp. 639-647 ◽  
Author(s):  
Abena S. Amoah ◽  
Benedicta B. Obeng ◽  
Irene A. Larbi ◽  
Serge A. Versteeg ◽  
Yvonne Aryeetey ◽  
...  
Keyword(s):  
Specific Ige ◽  
Cross Reactivity ◽  
Ige Antibodies ◽  
Specific Ige Antibodies

Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform

2008 ◽  
Vol 389 (4) ◽  
pp. 415-423 ◽  
Author(s):  
Susanne Riecken ◽  
Buko Lindner ◽  
Arnd Petersen ◽  
Uta Jappe ◽  
Wolf-Meinhard Becker
Keyword(s):  
Birch Pollen ◽  
Diagnostic Procedures ◽  
Cross Reactivity ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Reactive Protein ◽  
Bet V 1 ◽  
Peanut Extract ◽  
Natural Counterpart

Abstract The peanut allergen Ara h 8 is an important allergen for birch pollen allergic patients because of the cross-reactivity to the homologous Bet v 1. As the existence of Ara h 8 has been shown at the cDNA level so far (AY328088) and the allergen has indirectly been detected as natural protein, it was the aim of our study to identify natural Ara h 8 in peanut extract and to develop a purification strategy. This was achieved using a unique combination of purification steps, including optimized extraction conditions, size exclusion and ion exchange chromatography and treatment of the interfering contaminants with iodo-acetic acid. A characterization of the protein by microsequencing showed discrepancies to the deduced amino acid sequence of AY328088. For this reason, we cloned and expressed a new Ara h 8 isoform from cDNA (EU046325). This IgE-reactive protein corresponds to the results of microsequencing, ESI-FTICR-MS and trypsin fingerprinting analysis of the authentic and purified nAra h 8. Apart from the ultimate use of recombinant allergens for diagnostic procedures, there is also a scientific need for the natural counterpart, as it represents an excellent reference point by which to compare protein characteristics and to standardize diagnostic and therapeutic allergens.

scholarly journals An assessment of cross reactivity with patients allergic to birch pollen using the immunoblotting

2011 ◽  
Vol 1 (S1) ◽  
Author(s):  
Magdalena Zbikowska-Gotz ◽  
Andrzej Ku¿miñski ◽  
Jolanta JóŸwiak ◽  
Katarzyna Napiórkowska ◽  
Iwona Fares ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Cross Reactivity

The cross-reactivity of IgE antibodies with pollen allergens

1976 ◽  
Vol 58 (1) ◽  
pp. 129-139 ◽  
Author(s):  
Kristin M. Leiferman ◽  
Gerald J. Gleich
Keyword(s):  
Cross Reactivity ◽  
Pollen Allergens ◽  
Ige Antibodies ◽  
The Cross

Cross-reactivity of IgE antibodies to allergens

Allergy ◽  
2001 ◽  
Vol 56 (6) ◽  
pp. 478-490 ◽  
Author(s):  
R. C. Aalberse ◽  
J. Akkerdaas ◽  
R. van Ree
Keyword(s):  
Cross Reactivity ◽  
Ige Antibodies
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