Biochemical analysis demonstrates enhanced IgE binding of peach allergen Pru p 3 via selective fatty acid interactions, highlighting mechanisms driving severe plant food allergies.
Nonspecific lipid transfer proteins (nsLTPs) are major cross-reactive allergens identified in most plant-derived foods as well as pollen from diverse plants, and are often associated with severe symptoms in food allergy.1 Currently, Pru p 3 (major food allergen from peach [Prunus persica]) is regarded as the primary sensitizer for nsLTP-caused allergies.2 Pru p 3 shares the physicochemical characteristics of the nsLTP family. It is a small (9187 Da) basic protein, with a highly conserved 3-dimensional structure provided by 8 conserved cysteine residues forming 4 disulfide bridges.
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Dubiela et al. (2017) studied this question.
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