Pro j 2 is mesquite profilin: molecular characteristics and specific IgE binding activity

2014 ◽  
Keyword(s):  
Specific Ige ◽  
Binding Activity ◽  
Molecular Characteristics ◽  
Ige Binding

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.

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

Isolation and Characterization of a Relevant Aspergillus fumigatus Antigen with IgG- and IgE-Binding Activity

1988 ◽  
Vol 86 (2) ◽  
pp. 176-182 ◽  
Author(s):  
Viswanath P. Kurup ◽  
Muthiah Ramasamy ◽  
Paul A. Greenberger ◽  
Jordan N. Fink
Keyword(s):  
Aspergillus Fumigatus ◽  
Binding Activity ◽  
Isolation And Characterization ◽  
Ige Binding

scholarly journals SPADE web service for prediction of allergen IgE epitopes

2019 ◽  
Vol 47 (W1) ◽  
pp. W496-W501
Author(s):  
Fabio Dall’Antonia ◽  
Walter Keller
Keyword(s):  
Binding Sites ◽  
Specific Interaction ◽  
Epitope Prediction ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Machine Learning Algorithms ◽  
Training Data ◽  
Third Party ◽  
Prediction Methods ◽  
Ige Binding

Abstract The specific interaction of allergens with IgE antibodies and the allergen mediated cross-linking of receptor-bound IgE are key events of allergic diseases. The elucidation of the IgE binding sites (the epitopes) on the allergen surface is an important goal of allergy research. Only few allergen-specific IgE epitopes have been determined experimentally to date. Epitope prediction methods represent a viable alternative to experimental methods and have worked well with linear epitopes. However, as most IgE epitopes are of conformational and/or discontinuous nature sequence based prediction methods have had limited success in these cases. Here, we present the web server of the program SPADE (https://spade.uni-graz.at), which is the server implementation of a previously published program (1). In this approach we utilize the structural homology of cross-reactive allergens combined with the immunological cross-reactivity data for the discrimination of putative IgE-binding sites from non-cross-reactive surface patches. The method, although predictive, does not rely on machine-learning algorithms and does not require training data. The SPADE server features an easy-to-use interface, an automated pipeline consisting of third-party, as well as own, newly developed routines and a comprehensive output page.

scholarly journals Comparative study of the complement-activating and specific IgE-binding properties of ragweed pollen allergen

1997 ◽  
Vol 108 (1) ◽  
pp. 122-127 ◽  
Author(s):  
T. HIDVÉGI ◽  
L. BERRENS ◽  
L. VARGA ◽  
F. MARAÑON ◽  
B. SCHMIDT ◽  
...  
Keyword(s):  
Comparative Study ◽  
Specific Ige ◽  
Pollen Allergen ◽  
Ragweed Pollen ◽  
Binding Properties ◽  
Ige Binding
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