Abstract
Lectins or carbohydrate-binding proteins are widely distributed in seeds and vegetative parts of edible plant species. A few lectins from different fruits and vegetables have been identified as potential food allergens, including wheat agglutinin, hevein (Hev b 6.02) from the rubber tree and chitinases containing a hevein domain from different fruits and vegetables. However, other well-known lectins from legumes have been demonstrated to behave as potential food allergens taking into account their ability to specifically bind IgE from allergic patients, trigger the degranulation of sensitized basophils, and to elicit interleukin secretion in sensitized people. These allergens include members from the different families of higher plant lectins, including legume lectins, type II ribosome-inactivating proteins (RIP-II), wheat germ agglutinin (WGA), jacalin-related lectins, GNA (Galanthus nivalis agglutinin)-like lectins, and Nictaba-related lectins. Most of these potentially active lectin allergens belong to the group of seed storage proteins (legume lectins), pathogenesis-related protein family PR-3 comprising hevein and class I, II, IV, V, VI, and VII chitinases containing a hevein domain, and type II ribosome-inactivating proteins containing a ricin B-chain domain (RIP-II). In the present review, we present an exhaustive survey of both the structural organization and structural features responsible for the allergenic potency of lectins, with special reference to lectins from dietary plant species/tissues consumed in Western countries.
Highlights
Besides their beneficial effects on human health, the consumption of plant food products may cause some detrimental effects, mainly associated with the presence of toxic molecules and allergenic proteins, which often occur in various plant parts, including leaves, roots, bulbs, fruits, and seeds [1,2].the consumption of either crude or cooked foods from a variety of edible plant species is likely to trigger more or less severe allergic manifestations in both previously sensitized children and adults [3]
We present an exhaustive survey of both the structural organization and structural features responsible for the allergenic potency of lectins, with special reference to lectins from dietary plant species/tissues consumed in Western countries
The group of plant lectins comprise a huge number of proteins which share the common
Summary
Besides their beneficial effects on human health, the consumption of plant food products may cause some detrimental effects, mainly associated with the presence of toxic molecules and allergenic proteins, which often occur in various plant parts, including leaves, roots, bulbs, fruits, and seeds [1,2]. Among the protein allergens occurring in seeds and other vegetative tissues, the widely distributed plant lectins have been poorly investigated Their role as relevant food allergens still remains a matter of debate [13]. Different families of lectins with various carbohydrate-binding specificities, have been identified and characterized in detail in all living organisms Many of these lectins are rather abundant proteins in higher plants [14,15,16] (Table 1). IgE antibodies which most probably hampered the research in this area This shortcoming can be overcome by performing the IgE-binding experiments in the presence of a cocktail of inhibiting sugars, e.g., mannose + galactose, that prevent the non-specific binding of plant lectins to the carbohydrate moiety of IgE from sera of allergic patients [17].
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