Abstract

Here we focus our attention on the structural stability and physicochemical properties of plant nonspecific lipid-transfer proteins (nsLTPs) as keys to their allergenicity. We further present the current opinions on the route of sensitization and include the latest additions to the nsLTP allergen family. Plant nsLTPs are small cysteine-rich lipid-binding proteins that play a key role in plant resistance to biotic and abiotic stress. Besides their relevance for plant-pathogen interactions, nsLTPs have attracted interest as true food allergens which are of high importance to atopics in Mediterranean countries. It is now becoming clear that their molecular properties such as the remarkable stability to proteolysis and thermal denaturation are intrinsically linked to their allergenicity. These properties also facilitate sensitization via the gastrointestinal tract which allows these molecules to act as allergens independently of prior exposure to pollen. In addition, a group of allergenic pollen nsLTPs exists which seem to be only partially linked to the food nsLTPs by cross-reactivity. Research into the family of nsLTPs will continue to provide insights about the particular molecular properties that make an nsLTP an allergen and how primary sensitization occurs.

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