Cloning, expression, and immunological characterization of formosan subterranean termite (blattodea: rhinotermitidae) arginine kinase

Authors: Mattison, Chris; TUNGTRONGCHITR, ANCHALEE - Mahidol University; TILLE, KATHERINE - Malcolm Grow Medical Clinics And Surgical Center; COTTONE, CARRIE - New Orleans Mosquito, Termite & Rodent Control Board; RIEGEL, CLAUDIA - New Orleans Mosquito, Termite & Rodent Control Board

Submitted to: Journal of Insect Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/16/2020
Publication Date: 7/24/2020
Citation: Mattison, C.P., Tungtrongchitr, A., Tille, K.S., Cottone, C.B., Riegel, C. 2020. Cloning, expression, and immunological characterization of formosan subterranean termite (blattodea: rhinotermitidae) arginine kinase. Journal of Insect Science. Volume 20; Issue 4. https://doi.org/10.1093/jisesa/ieaa071.
DOI: https://doi.org/10.1093/jisesa/ieaa071

Interpretive Summary: Food and environmental allergies represent an increasing public health problem. Cockroaches, dust mites, and shrimp are considered significant sources of airborne or food allergens contributing to allergic disease in urban areas world-wide. Arginine kinase is an enzyme that has been demonstrated to commonly cause allergies. Arginine kinase enzymes from shrimp, moths, dust mite, and cockroaches are recognized by immunoglobulin-E (IgE) antibodies from allergic patients and can cause allergic reactions. Termites and cockroaches are evolutionarily related and share some behavioral similarities. Termites are a significant pest and typically live within and around urban centers, especially in the Southern United States. To determine if termite arginine kinase is also recognized by IgE, a recombinant version of the enzyme was made and purified. In testing with IgE from allergic volunteers the recombinant termite arginine kinase was also recognized by IgE from cockroach and shrimp allergic patients. This is the first study to demonstrate directly that a recombinant termite arginine kinase cross-reacts with IgE from both cockroach and shrimp allergic patients. These results suggest that termite arginine kinase may pose a threat to those with cockroach or shellfish allergies due to cross-reactivity, and may contribute as a sensitizing agent in geographic areas infested with termites.

Technical Abstract: Arthropod arginine kinase proteins are conserved proteins that can act as allergens across many species and are therefore commonly cross-reactive. The Formosan subterranean termite Coptotermes formosanus (C. formosanus) is in the order Blattodea and is closely related to cockroaches. In tropical and subtropical parts of the world C. formosanus is a common household pest. Previous research has indicated C. formosanus termites may contain IgE cross-reacting or allergenic proteins. In this study, C. formosanus termite extracts were screened for recognition by IgE from allergic volunteers. A band migrating at approximately 42kDa on SDS-PAGE from C. formosanus termite extracts cross-reacted with IgE from five cockroach allergic patient samples by immunoblot. Liquid chromatography-mass spectrometry analysis of gel slices from the corresponding region of a gel, indicated several peptides from the excised region were identical to the American cockroach arginine kinase allergen, Per a 9. The full-length sequence of the C. formosanus arginine kinase gene indicates the protein it encodes is 96% identical to American cockroach Per a 9, 94% identical to German cockroach Bla g 9, and 82-84% identical to shrimp arginine kinase proteins Pen m 2, Lit v 2, and Cra c 2. Full-length C. formosanus arginine kinase was fused to a glutathione S-transferase tag and recombinantly expressed and purified from Escherichia coli by affinity chromatography. The recombinant protein was recognized by IgE from 11 of 12 cockroach or shrimp allergic samples, but did not cross-react with dust mite allergic or peanut/tree nut allergic samples. The results of this study indicate the C. formosanus arginine kinase cross-reacts with cockroach and shrimp allergic IgE and has the potential to contribute allergic disease.