[HTML][HTML] The impact of nitration on the structure and immunogenicity of the major birch pollen allergen Bet v 1.0101

C Ackaert, S Kofler, J Horejs-Hoeck, N Zulehner… - PloS one, 2014 - journals.plos.org
Allergy prevalence has increased in industrialized countries. One contributing factor could
be pollution, which can cause nitration of allergens exogenously (in the air) or …

PLENARY LECTURES 39 BIOLOGICAL FUNCTIONS, ISOFORMS, AND ENVIRONMENTAL CONTROL IN THE BET v I GENE FAMILY

A Jilek¹, I Swoboda, H Breiteneder, I Fogy… - … and immunology of …, 1993 - books.google.com
Bet v I, the major allergen of birch pollen, is a 17 kD cytosolic protein that is quantitatively
extracted from pollen grains by simply washing with water. The cDNA sequence¹ of Bet v I …

NMR spectroscopy reveals common structural features of the birch pollen allergen Bet v 1 and the cherry allergen Pru a 1

K Schweimer, H Sticht, J Nerkamp, M Boehm… - Applied Magnetic …, 1999 - Springer
A high percentage of birch pollen allergic patients also experience food hypersensitivity
which results from common epitopes on the corresponding allergens. In order to analyze …

Mutational analysis of amino acid positions crucial for IgE-binding epitopes of the major apple (Malus domestica) allergen, Mal d 1

Y Ma, G Gadermaier, B Bohle, S Bolhaar… - International archives of …, 2005 - karger.com
Background: Individual amino acid residues of the major birch pollen allergen, Bet v 1, have
been identified to be crucial for IgE recognition. The objective of the present study was to …

Nasal challenges with recombinant derivatives of the major birch pollen allergen Bet v 1 induce fewer symptoms and lower mediator release than rBet v 1 wild‐type in …

M Van Hage‐Hamsten, E Johansson… - Clinical & …, 2002 - Wiley Online Library
Background Genetic engineering of the major birch pollen allergen (Bet v 1) has led to the
generation of recombinant Bet v 1 derivatives with markedly reduced IgE‐binding capacity …

[HTML][HTML] Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity

R Freier, E Dall, H Brandstetter - Scientific reports, 2015 - nature.com
Despite a high similarity with homologous protein families, only few proteins trigger an
allergic immune response with characteristic TH2 polarization. This puzzling observation is …

[HTML][HTML] Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen

Y Machado, R Freier, S Scheiblhofer… - Journal of Allergy and …, 2016 - Elsevier
Background The search for intrinsic factors, which account for a protein's capability to act as
an allergen, is ongoing. Fold stability has been identified as a molecular feature that affects …

Genetic engineering of a hypoallergenic trimer of the major birch pollen allergen, Bet v 1

S Vrtala, K Hirtenlehner, M Susani, M Akdis… - The FASEB …, 2001 - Wiley Online Library
An estimated 100 million individuals suffer from birch pollen allergy. Specific
immunotherapy, the only curative allergy treatment, can cause life‐threatening anaphylactic …

IgE and allergen‐specific immunotherapy‐induced IgG4 recognize similar epitopes of Bet v 1, the major allergen of birch pollen

N Groh, CS von Loetzen, B Subbarayal… - Clinical & …, 2017 - Wiley Online Library
Background Allergen‐specific immunotherapy (AIT) with birch pollen generates Bet v 1‐
specific immunoglobulin (Ig) G4 which blocks IgE‐mediated hypersensitivity mechanisms …

Birch pollen allergen Bet v 1 binds to and is transported through conjunctival epithelium in allergic patients

J Renkonen, P Mattila, S Lehti, J Mäkinen… - Allergy, 2009 - Wiley Online Library
Background: Previous work in type‐I pollen allergies has mainly focused on lymphocytes
and immune responses. Here, we begin to analyse with a systems biology view the …