Expression of Birch Pollen-Specific IgE-Binding Activity in Seeds and Other Plant Parts of Birch Trees (Betula verrucosa Ehrh.)

1992 ◽  
Vol 98 (4) ◽  
pp. 370-376 ◽  
Author(s):  
D.W. Fountain ◽  
B. Berggren ◽  
S. Nilsson ◽  
R. Einarsson
Keyword(s):  
Birch Pollen ◽  
Specific Ige ◽  
Binding Activity ◽  
Plant Parts ◽  
Ige Binding ◽  
Birch Trees ◽  
Betula Verrucosa

Quality and potency profile of eight recombinant isoallergens, largely mimicking total Bet v 1‐specific IgE binding of birch pollen

2019 ◽  
Vol 49 (5) ◽  
pp. 712-723 ◽  
Author(s):  
Christian Seutter von Loetzen ◽  
Andreas Reuter ◽  
Jelena Spiric ◽  
Thomas Schulenborg ◽  
Iris Bellinghausen ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Specific Ige ◽  
Bet V 1 ◽  
Ige Binding

scholarly journals Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: potential use of hypoallergenic isoforms for immunotherapy.

1996 ◽  
Vol 183 (2) ◽  
pp. 599-609 ◽  
Author(s):  
F Ferreira ◽  
K Hirtenlehner ◽  
A Jilek ◽  
J Godnik-Cvar ◽  
H Breiteneder ◽  
...  
Keyword(s):  
T Cell ◽  
T Lymphocytes ◽  
Birch Pollen ◽  
Binding Activity ◽  
Pollen Allergen ◽  
Type I ◽  
Bet V 1 ◽  
Ige Binding ◽  
Birch Pollen Allergen

We dissected the T cell activation potency and the immunoglobulin (Ig) E-binding properties (allergenicity) of nine isoforms of Bet v 1 (Bet v 1a-Bet v 1l), the major birch pollen allergen. Immunoblot experiments showed that Bet v 1 isoforms differ in their ability to bind IgE from birch pollen-allergic patients. All patients tested displayed similar IgE-binding patterns toward each particular isoform. Based on these experiments, we grouped Bet v 1 isoforms in three classes: molecules with high IgE-binding activity (isoforms a, e, and j), intermediate IgE-binding (isoforms b, c, and f), and low/no IgE-binding activity (isoforms d, g, and 1). Bet v 1a, a recombinant isoform selected from a cDNA expression library using IgE immunoscreening exhibited the highest IgE-binding activity. Isoforms a, b, d, e, and 1 were chosen as representatives from the three classes for experimentation. The potency of each isoallergen to activate T lymphocytes from birch pollen-allergic patients was assayed using peripheral blood mononuclear cells, allergen-specific T cell lines, and peptide-mapped allergen-specific T cell clones. Among the patients, some displayed a broad range of T cell-recognition patterns for Bet v 1 isoforms whereas others seemed to be restricted to particular isoforms. In spite of this variability, the highest scores for T cell proliferative responses were observed with isoform d (low IgE binder), followed by b, 1, e, and a. In vivo (skin prick) tests showed that the potency of isoforms d and 1 to induce typical urticarial type 1 reactions in Bet v 1-allergic individuals was significantly lower than for isoforms a, b, and e. Taken together, our results indicate that hypoallergenic Bet v 1 isoforms are potent activators of allergen-specific T lymphocytes, and Bet v 1 isoforms with high in vitro IgE-binding activity and in vivo allergenicity can display low T cell antigenicity. Based on these findings, we propose a novel approach for immunotherapy of type I allergies: a treatment with high doses of hypoallergenic isoforms or recombinant variants of atopic allergens. We proceed on the assumption that this measure would modulate the quality of the T helper cell response to allergens in vivo. The therapy form would additionally implicate a reduced risk of anaphylactic side effects.

Cross-Reactivity between IgE-Binding Proteins from Anisakis Simplex and Dermatophagoides Pteronyssinus

2005 ◽  
Vol 18 (4) ◽  
pp. 671-675 ◽  
Author(s):  
R. Bernardini ◽  
G. Mistrello ◽  
E. Novembre ◽  
D. Roncarolo ◽  
S. Zanotta ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Specific Ige ◽  
Dermatophagoides Pteronyssinus ◽  
Cross Reactivity ◽  
Anisakis Simplex ◽  
Cross Reaction ◽  
Ige Binding ◽  
Sds Page ◽  
The Cross

An association was found between Anisakis simplex (As) and Dermatophagoides pteronyssinus (Dp) sensitization. One recent study shows a cross-reactivity between As and Dp and tropomyosin (tr) is suspected as being one of the proteins responsible of this cross-reaction. The aim of our study was: 1) to confirm the cross-reactivity between Dp and As; 2) to determine the importance of tr in this cross reaction. SDS-PAGE analysis of Dp and As (metabolic and somatic) extracts was carried out. Then an IgE immunoblotting test using serum from a patient who had specific IgE only to Dp and As and immunoblotting inhibition experiments using Dp extract and tr as inhibitors were performed. We found that patient's serum reacted: 1) against larval As antigens with a molecular weight (mw) of 25 kilodalton (kD) and a mw > 100 kD, 2) against various metabolic As antigens with a mw > 100 kD, a mw ranging approximately from 35 to 50 kD, and a mw around 20 kD, and 3) against Dp proteins with mw between 35 and 55 kD. Preincubation of patient's serum with Dp extract caused the disappearance of reactivity against antigens with a mw > 100 kD in both larval and metabolic As extracts and against proteins with mw ranging approximately from 35 to 50 kD in the metabolic As extract. Preincubation of patient's serum with As extract caused the disappearance of reactivity against antigens with mw between 35 and 55 kD in the Dp extract. Pre-incubation of patient's serum with tr did not induce any change in the immunoblotting profile. The results show that 1) cross-reactive components between Dp and As are some proteins with a mw ranging approximately from 35 to 50 kD and with a mw > 100 kD, and 2) tr is not involved in cross-reactivity between As and Dp.

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