Date of Award
Open Access Dissertation
Chemistry and Biochemistry
Allergy is an outcome of an allergen-antibody reaction (1). Potent airborne allergens from dust mites and pets are major causative factors for allergic conditions among predisposed individuals. Group-2 allergen Der p 2 from Dermatophagoides pteronyssinus is a major allergen which causes allergic conditions in more than 80% of mite-allergic subjects (2). Similarly, airborne allergen Can f 1 from dog (Canis familiaris) is also a major risk allergen which affects 10-20% of the population worldwide (3). Considering the increasing prevalence of inhalant allergens in the environment, antigenic characterization is crucial for improving allergy diagnostics and management. This study focuses on the interaction of IgE, major inhalant allergens Der p 2, and Can f 1 by structural and immunological approaches. Here, we report three novel structures of Der p 2 and Can f 1 bound to human derived IgEs. Each structure was used as a basis to generate epitope-based mutants of Der p 2 and Can f 1. Mutants designed based on these crystal structures have shown reduced antibody binding and decreased anaphylactic response in a mouse model and hence can be potential candidates for house dust mite allergy immunotherapy (2). This research also explores the application of protein L in stabilizing recombinantly expressed antibody fragments for crystallographic purposes (4). We use protein L to crystalize antibody fragments, which have not been previously reported.
Khatri, K.(2023). Structural and Immunological Characterization of Inhaled Allergens and Their Complexes With Antibodies. (Doctoral dissertation). Retrieved from https://scholarcommons.sc.edu/etd/7166
Available for download on Thursday, May 15, 2025