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 α-amylase inhibitor family which are glycosylated, polypeptides 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 contains both β1←2 xylose and α1←3 fucose. Evidence is presented that the xylosyl residue and, to a lesser extent, the fucosyl residue are key IgE-binding epitopes and largely responsible for the allergenicity 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 the cross-reactivities often observed between pollen, vegetable food, and insect allergens.