Structural aspects of the allergen-antibody interaction

A Pomés, GA Mueller, M Chruszcz - Frontiers in immunology, 2020 - frontiersin.org
The development of allergic disease involves the production of IgE antibodies upon allergen
exposure in a process called sensitization. IgE binds to receptors on the surface of mast …

Immunotherapy of food allergy: a comprehensive review

CYY Wai, NYH Leung, PSC Leung, KH Chu - Clinical reviews in allergy & …, 2019 - Springer
Food allergy imposes a severe global health burden, and thus, there is a dire need for safe
and effective treatments. Allergen-specific immunotherapy (AIT) is currently the only …

Analysis of the allergenic epitopes of tropomyosin from mud crab using phage display and site-directed mutagenesis

GY Liu, XJ Mei, MJ Hu, Y Yang, M Liu… - Journal of Agricultural …, 2018 - ACS Publications
Mud crab (Scylla serrata), which is widely consumed, can cause severe allergic symptoms.
Eight linear epitopes and seven conformational epitopes of tropomyosin (TM) from S. serrata …

Still SDAPing along: 20 years of the structural database of allergenic proteins

CH Schein, SS Negi, W Braun - Frontiers in Allergy, 2022 - frontiersin.org
The introduction of plant extracts to mitigate the symptoms of “hay fever”, about a century
ago, led to discoveries beginning sixty years ago on determining the sequences and …

Conformational IgE epitopes of peanut allergens Ara h 2 and Ara h 6

X Chen, SS Negi, S Liao, V Gao… - Clinical & …, 2016 - Wiley Online Library
Summary Background Cross‐linking of IgE antibody by specific epitopes on the surface of
mast cells is a prerequisite for triggering symptoms of peanut allergy. IgE epitopes are …

Cross-React: a new structural bioinformatics method for predicting allergen cross-reactivity

SS Negi, W Braun - Bioinformatics, 2017 - academic.oup.com
The phenomenon of cross-reactivity between allergenic proteins plays an important role to
understand how the immune system recognizes different antigen proteins. Allergen proteins …

Kinetics, cross‐reactivity, and specificity of B et v 1‐specific I g G 4 antibodies induced by immunotherapy with birch pollen

B Subbarayal, D Schiller, C Möbs, NW de Jong… - Allergy, 2013 - Wiley Online Library
Background IgE antibodies specific for the major birch pollen allergen frequently cross‐react
with B et v 1 homologous food proteins, for example C or a 1 in hazelnut and Mal d 1 in …

Screening and identification of mimotopes of the major shrimp allergen tropomyosin using one-bead-one-compound peptide libraries

NYH Leung, CYY Wai, MHK Ho, R Liu… - Cellular & molecular …, 2017 - nature.com
The one-bead-one-compound (OBOC) combinatorial peptide library is a powerful tool to
identify ligand and receptor interactions. Here, we applied the OBOC library technology to …

Identification of Major B-Cell Linear Epitopes of Peach Allergen Pru p 3 Using Immune Slot-Blot Microarray Assay

W Kang, J Zhang, H Li, N Yu, R Tang… - Journal of Agricultural …, 2022 - ACS Publications
Pru p 3, one of the most representative proteins of the lipid transfer proteins (LTPs), is
responsible for clinical allergic reactions to food of peach origin. The identification of Pru p 3 …

Application of phage peptide display technology for the study of food allergen epitopes

X Chen, SC Dreskin - Molecular nutrition & food research, 2017 - Wiley Online Library
Phage peptide display technology has been used to identify IgE‐binding mimotopes (mimics
of natural epitopes) that mimic conformational epitopes. This approach is effective in the …