Relationship between the magnitude of IgE production in mice and conformational stability of the house dust mite allergen, Der p 2

• Published in: Biochimica et biophysica acta Vol. 1860; no. 10; pp. 2279 - 2284
• Main Authors: Nakamura, Hitomi, Ohkuri, Takatoshi, So, Takanori, Ueda, Tadashi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2016
• Subjects: ADAs (anti-drug antibodies); Allergen; allergens; Animals; antigen presentation; Antigen-Presenting Cells - immunology; Antigen-Presenting Cells - metabolism; Antigens, Dermatophagoides - chemistry; Antigens, Dermatophagoides - genetics; Antigens, Dermatophagoides - immunology; Arthropod Proteins - chemistry; Arthropod Proteins - genetics; Arthropod Proteins - immunology; blood serum; Conformational stability; denaturation; Der p 2; dust; dust mites; engineering; guanidines; Humans; immune response; Immunization; Immunogenicity; immunoglobulin E; Immunoglobulin E - blood; Immunoglobulin E - chemistry; Immunoglobulin E - immunology; major histocompatibility complex; Mice; Molecular Conformation; mutants; mutation; peptides; Protein Denaturation; proteinases; Pyroglyphidae - chemistry; Pyroglyphidae - immunology; T-lymphocytes; T-Lymphocytes - immunology; T-Lymphocytes - metabolism; vaccines; CD; Conformational stability; Der p 2; Immunogenicity; ADAs (anti-drug antibodies); Der p; HEL; Allergen

Protein antigens are degraded by endosomal protease in antigen presentation cell. T cells recognize peptides derived from antigen proteins bound to class II major histocompatibility complex molecules. We previously reported that an increase in the conformational stability of an antigen depressed its...