Plant seeds and tree nuts are responsible for the vast majority of food allergies. The prevalence of peanut and tree nut allergy has doubled among the children in the United States from 1997 to 2002, reaching 1.2% . Considerable research has been conducted to identify and characterize nut and seed allergens . Most of these allergens belong to the cupin and the prolamin superfamilies, but a new family, oleosin, has recently been identified . The first suspicion of oleosin involvement in allergy was reported more than 10 years ago , but awaited 2002 for formal evidence. Pons et al.  showed specific igE-binding with peanut oleosin in three of 14 sera of patients with allergic reaction to peanuts. Interestingly, the IgE binding was weak against oleosin monomers but stronger with proteins of HMW, presumed to be oleosin oligomers. The authors also argued for a possible cross-reactivity between oleosins from various seeds. More recently, oleosins were identified as allergens in two other seeds: sesame seed  and hazelnut . The IgEs of all studied patients with sesame allergy bound monomeric oleosins from purified sesame OB, but some of these patients had negative skin prick tests to aqueous sesame extracts. One hypothesis is that the highly hydrophobic oleosins are not present in aqueous seed extracts, due to their weak solubility in saline solutions. Moreover, several findings suggested that oleosins could be in peanut, soybean, and sesame oils and could be involved in allergic reactions to these oils [78, 79]. This raises the question of the quality of seed extracts used for diagnosis. This strongly supports the need of improving extraction and solubilization methods of hydrophobic proteins, together with their proteomics analysis, especially because some of these proteins (i.e., oleosin) recently appeared to be allergens.
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