Many plant proteins, particularly those found in foods and pollen, are
known to act as sensitizing agents in humans upon repeated exposure,
Among the cereal flour proteins involved in asthmatic reactions, those
members of the a-amylase inhibitor family which are glycosylated, pol
ypeptides BMAI-1, BTAI-CMb, and WTAI-CM16* are particularly reactive
both in vivo and in vitro, We show here that these major glycoprotein
allergens carry a single asparagine-linked complex glycan that contain
s both beta 1 --> 2 xylose and alpha 1 --> 3 fucose, Evidence is prese
nted that the xylosyl residue and, to a lesser extent, the fucosyl res
idue are key IgE-binding epitopes and largely responsible for the alle
rgenicity of these and unrelated proteins from plants and insects, Our
results suggest that the involvement of xylose- and fucose-containing
complex glycans in allergenic responses may have been underestimated
previously; these glycans provide a structural basis to help explain t
he cross-reactivities often observed between pollen, vegetable food, a
nd insect allergens.