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

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.

Molecular characterization of Dau c 1, the Bet v 1 homologous protein from carrot and its cross-reactivity with Bet v 1 and Api g 1

1999 ◽  
Vol 29 (6) ◽  
pp. 840-847 ◽  
Author(s):  
HOFFMANN-SOMMERGRUBER ◽  
O'RIORDAIN ◽  
AHORN ◽  
EBNER ◽  
DA CAMARA MACHADO ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Cross Reactivity ◽  
Homologous Protein ◽  
Bet V 1

Purification and characterization of natural Bet v 1 from birch pollen and related allergens from carrot and celery

2007 ◽  
Vol 51 (12) ◽  
pp. 1527-1536 ◽  
Author(s):  
Mirko A. Bollen ◽  
Aranzazu Garcia ◽  
Jan H. G. Cordewener ◽  
Harry J. Wichers ◽  
Johannes P. F. G. Helsper ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Purification And Characterization ◽  
Bet V 1

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
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