Official websites use. Share sensitive information only on official, secure websites. These authors have contributed equally to this work and share first authorship position. Background: Cross-reactivity between nonspecific lipid transfer proteins could cause anaphylaxis, further influencing food avoidance and nutrient deficiencies. The one affecting olive pollen Ole e 7 and peach Pru p 3 may underlie a variety of pollen-food syndromes, though a deep molecular analysis is necessary.
For epitope mapping, both digested proteins were incubated with patient sera, and the captured IgE-bound peptides were characterised by LC-MS. Results: The analysis revealed two Ole e 7 epitopes and the three Pru p 3 epitopes previously described. Although complete sequence alignment between both proteins revealed Conclusions: This study mapped sIgE-Ole e 7-binding epitopes, paving the way for more precise diagnostic tools.
Assuming non-significant sequence similarity, structural homology and shared key residues may underlie the potential cross-reactivity between Ole e 7 and Pru p 3 nsLTPs.
Keywords: food allergy, pollen-food syndrome, cross-reactivity, epitope mapping, Ole e 7 allergen, Pru p 3 allergen, nonspecific lipid transfer proteins nsLTPs. Food allergy is an aberrant, potentially life-threatening immune response induced by exposure to a harmless food antigen [ 1 ].
Food allergy represents a growing socioeconomic and public health problem, with an increasing prevalence in the last two decades. Worldwide, its prevalence is estimated to range from 0. Sensitisation to nonspecific lipid transfer proteins nsLTPs , particularly from the Rosaceae family, such as those in peaches, is becoming a clinical concern in Mediterranean countries, representing the most prevalent cause of food allergies [ 1 , 2 ].
