Utilization of Bet v 1 homologs based amplified profile (BBAP) variability in allergenic plants fingerprinting

Biologia ◽  
2022 ◽  
Author(s):  
Jana Žiarovská ◽  
Lucia Urbanová
Keyword(s):  
Bet V 1 ◽  
Allergenic Plants

scholarly journals Molecular characterization of recombinant T1, a non-allergenic periwinkle (Catharanthus roseus) protein, with sequence similarity to the Bet v 1 plant allergen family

2003 ◽  
Vol 373 (1) ◽  
pp. 261-269 ◽  
Author(s):  
Sylvia LAFFER ◽  
Said HAMDI ◽  
Christian LUPINEK ◽  
Wolfgang R. SPERR ◽  
Peter VALENT ◽  
...  
Keyword(s):  
Catharanthus Roseus ◽  
Sequence Similarity ◽  
Immunogold Electron Microscopy ◽  
Type I ◽  
Skin Reactions ◽  
Bet V 1 ◽  
Allergenic Plants ◽  
Ige Mediated

More than 25% of the population suffer from Type I allergy, an IgE-mediated hypersensitivity disease. Allergens with homology to the major birch (Betula verrucosa) pollen allergen, Bet v 1, belong to the most potent elicitors of IgE-mediated allergies. T1, a cytokinin-inducible cytoplasmic periwinkle (Catharanthus roseus) protein, with significant sequence similarity to members of the Bet v 1 plant allergen family, was expressed in Escherichia coli. Recombinant T1 (rT1) did not react with IgE antibodies from allergic patients, and failed to induce basophil histamine release and immediate-type skin reactions in Bet v 1-allergic patients. Antibodies raised against purified rT1 could be used for in situ localization of natural T1 by immunogold electron microscopy, but did not cross-react with most of the Bet v 1-related allergens. CD analysis showed significant differences regarding secondary structure and thermal denaturation behaviour between rT1 and recombinant Bet v 1, suggesting that these structural differences are responsible for the different allergenicity of the proteins. T1 represents a non-allergenic member of the Bet v 1 family that may be used to study structural requirements of allergenicity and to engineer hypo-allergenic plants by replacing Bet v 1-related allergens for primary prevention of allergy.

Quantification in mass units of Bet v 1, the main allergen of Betula verrucosa pollen, by a monoclonal antibody based-ELISA

1997 ◽  
Vol 27 (8) ◽  
pp. 926-931 ◽  
Author(s):  
J. RAMiREZ ◽  
J. A. CARPIZO ◽  
H. IPSEN ◽  
J. CARREIRA ◽  
M. LOMBARDERO
Keyword(s):  
Monoclonal Antibody ◽  
Bet V 1 ◽  
Betula Verrucosa

scholarly journals Bet v 1 from birch pollen is a hypoallergen with vitamin D3 in the pocket

Allergy ◽  
2021 ◽  
Author(s):  
Karin Hufnagl ◽  
Livia Kromp ◽  
Rodolfo Bianchini ◽  
Sheriene Moussa Afify ◽  
Markus Wiederstein ◽  
...  
Keyword(s):  
Vitamin D3 ◽  
Birch Pollen ◽  
Bet V 1

Epicutaneous immune modulation with Bet v 1 plus R848 suppresses allergic asthma in a murine model

Allergy ◽  
2013 ◽  
Vol 69 (3) ◽  
pp. 328-337 ◽  
Author(s):  
S. Siebeneicher ◽  
S. Reuter ◽  
M. Krause ◽  
A. Wangorsch ◽  
J. Maxeiner ◽  
...  
Keyword(s):  
Allergic Asthma ◽  
Murine Model ◽  
Immune Modulation ◽  
Bet V 1

scholarly journals Caveolar transport through nasal epithelium of birch pollen allergen Bet v 1 in allergic patients

2009 ◽  
Vol 124 (1) ◽  
pp. 135-142.e21 ◽  
Author(s):  
Sakari Joenväärä ◽  
Pirkko Mattila ◽  
Jutta Renkonen ◽  
Antti Mäkitie ◽  
Sanna Toppila-Salmi ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Pollen Allergen ◽  
Nasal Epithelium ◽  
Bet V 1 ◽  
Birch Pollen Allergen

Immunologic significance of respirable atmospheric starch granules containing major birch allergen Bet v 1

Allergy ◽  
1999 ◽  
Vol 54 (5) ◽  
pp. 478-483 ◽  
Author(s):  
GF Schäppi ◽  
PE Taylor ◽  
IA Staff ◽  
JM Rolland ◽  
C Suphioglu
Keyword(s):  
Starch Granules ◽  
Bet V 1

scholarly journals Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen

2004 ◽  
Vol 385 (1) ◽  
pp. 319-327 ◽  
Author(s):  
Regina WICHE ◽  
Michaela GUBESCH ◽  
Herbert KÖNIG ◽  
Kay FÖTISCH ◽  
Andreas HOFFMANN ◽  
...  
Keyword(s):  
Food Allergy ◽  
Amino Acid ◽  
Prunus Avium ◽  
Protein Structures ◽  
Cross Reactivity ◽  
Type I ◽  
Binding Region ◽  
Leukaemia Cell Line ◽  
Bet V 1 ◽  
Ige Binding

Birch (Betula verrucosa) pollen-associated food allergy is a well-characterized syndrome, which is due to the cross-reactivity of IgE antibodies to homologous allergens in various foods. One crossreacting area on the major birch pollen allergen Bet v 1 and its homologue in cherry (Prunus avium) Pru av 1 has already been identified. This is the so-called ‘P-loop’ region, which encompasses amino acid residues around position 45 and is found on the two virtually identical tertiary protein structures. We tried to determine an additional IgE cross-reacting patch on Pru av 1 and Bet v 1. The putative IgE-binding region on Pru av 1 was localized with a mAb (monoclonal antibody) that was generated against Bet v 1, and cross-reacts with several Bet v 1 homologues in food and inhibits the binding of patients' IgE to Pru av 1. mAb reactivity pattern was analysed and amino acid positions 28 and 108 of Pru av 1 were selected and mutated by site-directed mutagenesis. The Pru av 1 mutants were produced as recombinant proteins and characterized for their folding, mAb- and IgE-binding capacity and allergenic potency with a cellular assay using the humanized rat basophilic leukaemia cell line RBL-25/30. Amino acid position 28 is involved in a second major IgE-binding region on Pru av 1 and probably on Bet v 1. The identification of this second major IgE-binding region is an essential prerequisite to understand the phenomenon of cross-reactivity and its clinical consequences, and to produce hypoallergenic proteins for an improved immunotherapy of type I allergy.

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