Human IgE monoclonal antibody recognition of mite allergen Der p 2 defines structural basis of an epitope for IgE cross-linking and anaphylaxis in vivo

• Published in: PNAS nexus Vol. 1; no. 3; p. pgac054
• Main Authors: Khatri, Kriti, Richardson, Crystal M, Glesner, Jill, Kapingidza, Anyway Brenda, Mueller, Geoffrey A, Zhang, Jian, Dolamore, Cole, Vailes, Lisa D, Wünschmann, Sabina, Peebles, R Stokes, Chapman, Martin D, Smith, Scott A, Chruszcz, Maksymilian, Pomés, Anna
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.07.2022
• Subjects: Ablation; Allergens; Allergies; Amino acids; Anaphylaxis; Antigenic determinants; B cells; Biological, Health, and Medical Sciences; Crosslinked polymers; Crosslinking; Crystal structure; Crystals; Development and progression; Epitopes; Health aspects; Histamine; House dust; Hydrogen bonding; Immune response; Immunoglobulin E; Leukocytes (basophilic); Light chains; Lymphocytes B; Mast cells; Mites; Monoclonal antibodies; Proteins; Structure; United States; IgE antibody; allergy; anaphylaxis; allergen–antibody interaction; house dust mite

Immunoglobulin E (IgE) antibody is a critical effector molecule for adaptive allergen-induced immune responses, which affect up to 40% of the population worldwide. Allergens are usually innocuous molecules but induce IgE antibody production in allergic subjects. Allergen cross-linking of IgE bound t...