Abstract

RATIONALE: Ara h 2 is comparatively resistant to digestion and a digestion-resistant peptide (DRP-Ara h 2) is released in model digestion experiments. The presence of intact peanut protein and/or DRP-Ara h 2 in serum and saliva of humans after ingestion of peanut might help in assessing the risk of an allergic reaction to saliva from kissing or use of shared utensils. METHODS: Ten healthy, non-allergic volunteers (ages 19-50) consumed capsules containing a total of 25 gm of roasted peanut flour (12.75 gm protein). Two additional volunteers, serving as negative controls, consumed capsules containing 25 gm of powdered sugar. Blood and saliva samples were collected at baseline and at various time points up to 24 hours after ingestion. Levels of intact peanut proteins were measured over time using a commercial peanut ELISA. Levels of DRP-Ara h 2 in similar fluids were measured using a uniquely developed inhibition ELISA. RESULTS: DRP-Ara h 2 was detected in the serum of 9 of 10 volunteers (maximum of 248 ng DRP-Ara h 2/ml serum) and in the saliva of 7 of 10 volunteers (maximum of 4890 ng DRP-Ara h 2/ml saliva) for up to 24 hours after ingestion. Intact peanut protein was not detected in either serum or saliva throughout all collection time points. CONCLUSIONS: Demonstration of the stability and distribution of digestion resistant peanut allergens in human body fluids over an extended period of time may provide insight into potential risks posed by exposure to allergenic proteins in saliva.

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