Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core  1,3-linked fucose and xylose substitutions

Abstract

The N-glycans from 27 "plant" foodstuffs, including one from a gymnospermic plant and one from a fungus, were prepared by a new procedure and examined by means of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). For several samples, glycan structures were additionally investigated by size-fractionation and reverse-phase high-performance liquid chromatography in conjunction with exoglycosidase digests and finally also (1)H-nuclear magnetic resonance spectroscopy. The glycans found ranged from the typical vacuolar "horseradish peroxidase" type and oligomannose to complex Le(a)-carrying structures. Though the common mushroom exclusively contained N-glycans of the oligomannosidic type, all plant foods contained mixtures of the above-mentioned types. Apple, asparagus, avocado, banana, carrot, celery, hazelnut, kiwi, onion, orange, pear, pignoli, strawberry, and walnut were particularly rich in Le(a)-carrying N-glycans. Although traces of Le(a)-containing structures were also present in almond, pistachio, potato, and tomato, no such glycans could be found in cauliflower. Coconut exhibited almost exclusively N-glycans containing only xylose but no fucose. Oligomannosidic N-glycans dominated in buckwheat and especially in the legume seeds mung bean, pea, peanut, and soybean. Papaya presented a unique set of hybrid type structures partially containing the Le(a) determinant. These results are not only compatible with the hypothesis that the carbohydrate structures are another potential source of immunological cross-reaction between different plant allergens, but they also demonstrate that the Le(a)-type structure is very widespread among plants.

Engineering and evaluation of a mouse/human chimeric antibody against Shiga toxin 2

“…In this study, the deduced rS2C4-IgG1level is about 24 mg per liter (data not shown), with a good balance of heavy/light chains expression ( Figure 1C). The insect cell has a different post translational glycoprotein pattern from mammalian hosts (Wilson et al, 2001). However, many studies have reported that these differences do not affect IgG activities (Boyd et al, 1995), consistent with our results that rS2C4-IgG1 exerted in vitro and in vivo functions similar to its parent antibody.…”

Enhancement of fruit shelf life by suppressingN-glycan processing enzymes

“…Lectin blotting (SI Materials and Methods) was performed using wheat germ agglutinin (binds to GlcNAc; Sigma) or G. nivalis agglutinin (binds to mannose; Roche). Glycoprotein-linked N-glycans and free N-glycans were isolated as described previously (37,38), with few modifications (SI Materials and Methods).…”

Coping with cross-reactive carbohydrate determinants in allergy diagnosis

“…Second, peanut glycoproteins contain almost no fucose [14]. Anti-Xyl IgE never found above baseline -even in peanut allergic patients [Eiwegger T, Altmann F, Vienna, Austria; unpublished results].…”