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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #367912

Research Project: Reducing Peanut and Tree Nut Allergy

Location: Food Processing and Sensory Quality Research

Title: Cross-reaction of Formosan termite (Coptotermes formosanus) arginine kinase with and cockroach Per a 9

item Mattison, Chris

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 7/1/2019
Publication Date: N/A
Citation: N/A

Interpretive Summary: The incidence of food allergies appears to be increasing and is a serious public health concern. Shellfish are considered a major class of food allergens and cockroaches are considered a major class of airborne allergens. Allergens from shrimp and cockroaches, such as the arginine kinase protein, cross-react and contribute to the incidence of allergic disease. The American cockroach arginine kinase protein is termed Per a 9, is widespread, and can give rise to respiratory symptoms, oral allergy, and food allergy symptoms in sensitive individuals. Cockroaches and termites are closely related evolutionarily within the same order (Blattodea) and they share some behavioral similarities that can give rise to human-termite interaction. Gene sequencing and proteomic analysis indicates a termite arginine kinase protein can cross-react with cockroach and shrimp allergens. Whole termite extracts containing termite arginine kinase reacted with anti-cockroach allergen IgG and human IgE antibodies from serum samples of cockroach allergic patients. A recombinant termite arginine kinase protein made in bacteria is also recognized by IgG and human IgE antibodies. This is the first study to demonstrate directly that native and recombinant termite arginine kinase cross-reacts with IgE from cockroach allergic patients. These results suggest that termite arginine kinase may pose a threat to those with cockroach, shrimp, or other arthropod allergies due to cross-reactivity, and may contribute as a sensitizing agent in geographic areas infested with termites. The findings from this study could be applied to development of molecular chimeras with unique and informative epitopes, development of potentially therapeutic hypo-allergens, advances in epitope analysis, and application to clinical studies.

Technical Abstract: Arthropod arginine kinase proteins are considered pan-allergens and they are commonly cross-reactive. The Formosan subterranean termite Coptotermes formosanus (C. formosanus) is closely related to cockroaches in the order Blattodea and is a common household pest in tropical and subtropical parts of the world. A band migrating around 42kDa 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 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 1, 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.