Plant lipid transfer proteins, a widespread family of proteins, have been r
ecently identified as important food allergens. Their common structural fea
tures, such as eight conserved cysteines forming disulfide bridges, basic i
soelectric point and high similarity in amino acid sequence, are the basis
of allergic clinical crossreactivity. This has been demonstrated for the LT
P allergens of the Prunoideae subfamily, whose similarity is about 95% as d
emonstrated for the purified allergens of peach, apricot, plum and apple. A
relevant aspect is the existence of sequence homology of LTPs of botanical
ly unrelated foods, as demonstrated for LTPs of maize and peach. A class of
food allergens of well recognized clinical importance is that of seed stor
age 2S albumins. They have been identified in the most diffused edible seed
s and nuts, such as mustard, sesame, Brazil nut, walnut and peanut. In part
icular, a strong correlation between IgE-binding to these proteins and food
-induced anaphylaxis has been demonstrated for Brazil nut and sesame seeds.