Date of Award
Open Access Dissertation
Chemistry and Biochemistry
Allergies throughout the world are increasing in prevalence and severity. Although the direct causes of the development of allergies are not confirmed, study of proteins that cause reactions will lead to a deeper understanding of allergy. This work focuses on three panallergen families, profilins, parvalbumins, and arginine kinases, to further elucidate the background of allergy from the point of view of the allergens themselves. In Chapter 1, we evaluate pollen, fruit, and mite profilins in the context of allergy, showing the relevance of conserved cysteine residues in stability and oligomerization as well as the first data on cross-reactivity between plant and mite profilins. Chapter 2 continues the discussion of profilins with their use as a protein model for covalent modification of exposed and buried cysteines. Chapter 3 discusses parvalbumins, which are considered to be the major fish allergen; we show novel structures as well as evaluate the reliance on calcium for stability. Finally, Chapter 4 and 5 discuss arginine kinases, focusing first on their varied allergenicity and possible cross-reactivity, and continuing with an evaluation of their ligand binding and structural variation. We have characterized many proteins from these three families in terms of their biochemical properties, structures, and immunological relevance with the goal of leading to answers of why many proteins are allergens and why some induce more potent reactions than others, as well as give further insight into the relevance of cross-reactivity between similar allergens.
O'Malley, A. L.(2023). Biochemical, Structural, and Immunological Characterization of Selected Panallergens. (Doctoral dissertation). Retrieved from https://scholarcommons.sc.edu/etd/7184
Available for download on Thursday, May 15, 2025