scholarly journals Dominant Epitopes and Allergic Cross-Reactivity: Complex Formation Between a Fab Fragment of a Monoclonal Murine IgG Antibody and the Major Allergen from Birch Pollen Bet v 1

2000 ◽  
Vol 165 (1) ◽  
pp. 331-338 ◽  
Author(s):  
Osman Mirza ◽  
Anette Henriksen ◽  
Henrik Ipsen ◽  
Jørgen N. Larsen ◽  
Margit Wissenbach ◽  
...  
Keyword(s):  
Complex Formation ◽  
Birch Pollen ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Igg Antibody ◽  
Fab Fragment ◽  
Bet V 1

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.

Ara h 8, a Bet v 1–homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy

2004 ◽  
Vol 114 (6) ◽  
pp. 1410-1417 ◽  
Author(s):  
Diana Mittag ◽  
Jaap Akkerdaas ◽  
Barbara K. Ballmer-Weber ◽  
Lothar Vogel ◽  
Marjolein Wensing ◽  
...  
Keyword(s):  
Peanut Allergy ◽  
Birch Pollen ◽  
Major Allergen ◽  
Bet V 1

Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1–related food allergens

2005 ◽  
Vol 116 (1) ◽  
pp. 213-219 ◽  
Author(s):  
Beatrice Jahn-Schmid ◽  
Astrid Radakovics ◽  
Dirk Lüttkopf ◽  
Stephan Scheurer ◽  
Stefan Vieths ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Epitope ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Pollen Allergen ◽  
T Cell Epitope ◽  
Food Allergens ◽  
Bet V 1 ◽  
Birch Pollen Allergen

Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab′ fragment

1999 ◽  
Vol 55 (12) ◽  
pp. 2035-2036 ◽  
Author(s):  
Michael D. Spangfort ◽  
Osman Mirza ◽  
L. Anders Svensson ◽  
Jørgen N. Larsen ◽  
Michael Gajhede ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Birch Pollen ◽  
Pollen Allergen ◽  
Structural Basis ◽  
Type I ◽  
X Rays ◽  
Fab Fragment ◽  
Cell Parameters ◽  
Bet V 1 ◽  
Birch Pollen Allergen

The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen–antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab′ fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 Å, α = 105.7, β = 98.32, γ = 97.62°, and diffract to 2.9 Å resolution when analyzed at 100 K using synchrotron-generated X-rays.

scholarly journals Cross-reactivity of birch anthers and leaves with birch pollen antigens and allergens. A fine-structural immunocytochemical study using the post-embedding protein-A-gold technique.

1986 ◽  
Vol 34 (11) ◽  
pp. 1459-1464 ◽  
Author(s):  
M Grote ◽  
H G Fromme
Keyword(s):  
Binding Sites ◽  
Protein A ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Anther Wall ◽  
Cell Organelles ◽  
Igg Antibody ◽  
Thin Sections ◽  
Antibody Preparation ◽  
Rabbit Igg

Ultra-thin sections of vegetative tissues from birch (anthers and leaves) were labeled for pollen antigens and allergens using a commercial rabbit IgG antibody preparation directed against birch pollen antigens and allergens. Antibody binding sites were visualized using the protein A-gold technique. Specific labeling occurred in anther tissue (tape-tum cells, anther wall cells) as well as in the birch leaf (assimilation parenchyma). In both types of tissue, antigens and allergens were detected throughout the living protoplast (including cell organelles such as nuclei, mitochondria, and plastids). The cellulose cell walls were always free from anti-birch-pollen IgG-binding sites. The immunological controls (normal rabbit IgG) showed a low degree of nonspecific labeling. In plant tissues belonging to genera quite different from birch (tulip anther, rhododendron leaves), after incubation with the specific IgG weak labeling was observed. The immunological basis for these results is discussed.

Kinetics, cross-reactivity, and specificity of Bet v 1-specific IgG4 antibodies induced by immunotherapy with birch pollen

Allergy ◽  
2013 ◽  
Vol 68 (11) ◽  
pp. 1377-1386 ◽  
Author(s):  
B. Subbarayal ◽  
D. Schiller ◽  
C. Möbs ◽  
N. W. de Jong ◽  
C. Ebner ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Cross Reactivity ◽  
Bet V 1 ◽  
Specific Igg4

Purification and Characterization of the Major Allergen from Apple and Its Allergenic Cross-Reactivity with Bet v 1

1995 ◽  
Vol 108 (2) ◽  
pp. 119-126 ◽  
Author(s):  
Barbel Fahlbusch ◽  
Olga Rudeschko ◽  
W.D. Müller ◽  
G. Schlenvoigt ◽  
S. Vettermann ◽  
...  
Keyword(s):  
Major Allergen ◽  
Cross Reactivity ◽  
Purification And Characterization ◽  
Bet V 1

IgE and allergen-specific immunotherapy-induced IgG4recognize similar epitopes of Bet v 1, the major allergen of birch pollen

2016 ◽  
Vol 47 (5) ◽  
pp. 693-703 ◽  
Author(s):  
N. Groh ◽  
C. S. von Loetzen ◽  
B. Subbarayal ◽  
C. Möbs ◽  
L. Vogel ◽  
...  
Keyword(s):  
Specific Immunotherapy ◽  
Birch Pollen ◽  
Major Allergen ◽  
Allergen Specific Immunotherapy ◽  
Bet V 1

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.

Sign in / Sign up

Export Citation Format

Share Document