ARS | Publication request: Cross-reactivity of termite myosin; a potential allergen

Submitted to: Internet Web Page
Publication Type: Research Notes
Publication Acceptance Date: September 17, 2011
Publication Date: September 17, 2011
Citation: Mattison, C.P., Tarver, M.R., Florane, C.B. 2011. Cross-reactivity of termite myosin; a potential allergen. AB CAM Internet Web Page.

Interpretive Summary: Identifying and characterizing allergens is important for the protection of human health and preservation of quality of life. Myosin is a common food allergen found in foods; such as, shrimp, lobster, and crab. Identifying and characterizing proteins in similar species is often helpful for understanding why some food proteins cause allergy, while very similar proteins do not. Termites and other arthropods have almost identical myosin proteins as their shellfish relatives. By characterizing the termite myosin protein, we can gain a better understanding of the unique qualities of shellfish myosin proteins, and potentially gain insights into the mechanisms that cause allergic reactions in humans. In this research, we tested the reactivity of termite myosin using a commercially available anti-myosin antibody from the flight muscle of the waterbug. We found that the antibody recognized protein bands that have the expected size of myosin. This new tool allows us to identify and characterize the expression pattern of this important food-allergy protein in termites.

Technical Abstract: Myosin and myosin isoforms are common food allergens in crustaceans; such as, shrimp, lobster, and crab. Allergy to Shellfish is a prevalent and potentially long lasting disorder that can severely affect health and quality of life. Myosin and myosin isoforms of dust mites and cockroaches are similar to shellfish myosins, and are also found to be common household allergens. Household insect allergens can help to sensitize children to food allergies and may complicate food allergy symptoms. There is similarity among cockroach and termite myosin sequences, and it is possible that termite myosins may also be an important household allergen in areas of the country where termites are prevalent. In order to find molecular tools to characterize termite myosins, we evaluated the ability of a commercial insect myosin antibody to recognize termite myosin. We tested the cross-reactivity of termite myosin using the anti-myosin antibody (Abcam [MAC147], ab51098) from the flight muscle of Waterbug (Lethocerus indicus) in termite extracts. We find that this antibody recognizes protein bands consistent with the size and expression pattern of termite myosin. This new tool allows us to follow myosin expression in termites and will help to evaluate termite myosin as a possible household allergen.