Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

D Apostolovic, D Stanic-Vucinic, HHJ De Jongh… - Scientific reports, 2016 - nature.com
Conglutins represent the major peanut allergens and are renowned for their resistance to
gastro-intestinal digestion. Our aim was to characterize the digestion-resistant peptides …

[HTML][HTML] Retinoic acid‐loading of the major birch pollen allergen Bet v 1 may improve specific allergen immunotherapy: in silico, in vitro and in vivo data in BALB/c …

K Hufnagl, SM Afify, N Braun, S Wagner, M Wallner… - Allergy, 2020 - ncbi.nlm.nih.gov
To the Editor, More than twenty different isoforms of Bet v 1, the major birch pollen allergen,
have been identified, sharing an amino acid sequence identity of 95% and an almost …

Insights into the immune manipulation mechanisms of pollen allergens by protein domain profiling

S Patel, A Rani, A Goyal - Computational Biology and Chemistry, 2017 - Elsevier
Plant pollens are airborne allergens, as their inhalation causes immune activation, leading
to rhinitis, conjunctivitis, sinusitis and oral allergy syndrome. A myriad of pollen proteins …

Random mutagenesis and phage display technology as a tool for identifying ige epitopes of the birch pollen allergen Bet v 1

EE Guhsl, G Hofstetter, C Ebner, W Hemmer… - Clinical and …, 2014 - Springer
Background IgE-binding epitopes of the major birch pollen allergen Bet v 1 are dependent
on the native structure of the allergen. To date, only a single IgE epitope has been identified …

[HTML][HTML] The molecular basis of allergenicity: comparative analysis of the three dimensional structures of diverse allergens reveals a common structural motif

R Furmonaviciene, F Shakib - Molecular Pathology, 2001 - ncbi.nlm.nih.gov
Background—Although a large number of allergens have been characterised, the structural,
functional, and biochemical features that these molecules have in common, and that could …

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 …

Top‐down and bottom‐up characterization of nitrated birch pollen allergen Bet v 1a with CZE hyphenated to an Orbitrap mass spectrometer

S Gusenkov, H Stutz - Electrophoresis, 2018 - Wiley Online Library
Tyrosine (Tyr) residues of the major pollen allergen of birch Betula verrucosa, Bet v 1a, were
nitrated by peroxynitrite. This modification enhances the allergenicity. Modified tyrosines …

Comparative molecular modelling identifies a common putative IgE epitope on cysteine protease allergens of diverse sources

Furmonaviciene, Sewell, Shakib - Clinical & Experimental …, 2000 - Wiley Online Library
Background Previous approaches for studying common allergenic epitopes have mainly
focused on sequence comparisons, which unfortunately yield little or no information on the …

Harmonization of the genetic code effectively enhances the recombinant production of the major birch pollen allergen bet v 1

C Asam, A Roulias, MA Parigiani, A Haab… - … Archives of Allergy and …, 2018 - karger.com
Background: Enhancing the quality and yield of protein production in heterologous
expression systems is an important issue for developing new biopharmaceuticals. It has …

Evidence for an alpha helical T cell epitope in the C-terminus of the main birch pollen allergen Bet V 1

AJ Kungl, M Susani, A Lindemann, M Machius… - Biochemical and …, 1996 - Elsevier
Secondary structure prediction of the main birch pollen allergen Bet v 1 was found to be in
good agreement with the secondary structural elements found by analysing the Bet v 1 …