Arginine kinase (AK) from the phosphagen kinase family is a cross-reactive shellfish allergen. Structurally related cross-reactive allergens are involved in the pathogenesis of allergic symptoms. This study aimed to unravel the cross-reactivity of AK from a structural perspective. The crystal structure of Procambarus clarkii AK (Pro c 2) was resolved at 1.57 Å resolution, which showed a well-conserved structure not only to shellfish AKs but also to fish creatine kinase (CK), another allergen from the phosphagen kinase family. In Western blot, the CK corresponding protein in fish muscles was found to be reactive with AK-specific immunoglobulin (Ig) G. Recombinant Pro c 2 (rPro c 2) and CKs from Lateolabrax japonicus (rCK-L) and Ctenopharyngodon idell (rCK-C) were then produced, and the IgE reactivity of rCK-L and rCK-C, as well as their IgG/IgE cross-reactivity with rPro c 2, was confirmed by immunological assays. This study demonstrated the cross-reactivity among aquatic allergens from the phosphagen kinase family due to their structural similarity.
Keywords: allergen; aquatic allergy; arginine kinase; creatine kinase; cross-reactivity; crystal structure; phosphagen kinase family.