Cross-Reactions between Vegetable Foods, Pollen and Bee Venom Due to IgE Antibodies to a Ubiquitous Carbohydrate Determinant

Aalberse, R. C.; Koshte, V. L.; Clemens, J.G.J.

doi:10.1159/000232913

Cited by 41 publications

(21 citation statements)

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“…Cross-reactions in immunoassays of plant, arthropod and mollusk extracts have been reported for a number of years, in particular a "carbohydrate cross-reacting determinant" has been hypothesized but not structurally analyzed (Aalberse et al, 1981a). IgE and/or IgG reactivity against the carbohydrate moieties of Lol p XI (an antigen from the pollen of ryegrass, Lolium perenne) (van Ree et al, 1995a), Olea europaea (de Cesare et al, 1993), as well as specifically the major olive pollen allergen Ole e I (Batanero et al, 1994(Batanero et al, , 1996, Cry j I (an allergen from the pollen of Cryptomeria japonica, Japanese cedar) (Hijikata et al, 1994), buckwheat (Aalberse et al, 1981b), Parietaria judaica (Mucci et al, 1992), Bermuda grass BG60 allergen , tomato fruit and grass pollen (Petersen et al, 1996), cereal flour (Garcia-Casado et al, 1996), and a hydroxyproline-rich glycoprotein from Parthenium hysterophorus pollen (Gupta et al, 1996) has been proposed on the basis of reduction of reactivity after chemical deglycosylation or retention of inhibition of immunoassays after protease treatment.…”

Section: Introductionmentioning

confidence: 99%

Core 1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts

Wilson¹,

et al. 1998

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683Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts Carbohydrates have been suggested to account for some IgE cross-reactions between various plant, insect, and mollusk extracts, while some IgG antibodies have been successfully raised against plant glycoproteins. A rat monoclonal antibody raised against elderberry abscission tissue (YZ1/2.23) and rabbit polyclonal antiserum against horseradish peroxidase were screened for reactivity in enzyme-linked immunosorbent assay against a range of plant glycoproteins and extracts as well as neoglycoproteins, bee venom phospholipase, and several animal glycoproteins. Of the oligosaccharides tested, Man 3 XylFucGlcNAc 2 (MMXF 3 ) derived from horseradish peroxidase was the most potent inhibitor of the reactivity of both YZ1/2.23 and anti-horseradish peroxidase to native horseradish peroxidase glycoprotein. The reactivity of YZ1/2.23 and anti-horseradish peroxidase against Sophora japonica lectin was most inhibited by a neoglycoconjugate of bromelain glycopeptide cross-linked to bovine serum albumin, while the defucosylated form of this conjugate was inactive as an inhibitor. A wide range of plant extracts was found to react against YZ1/2.23 and anti-horseradish peroxidase, with particularly high reactivities recorded for grass pollen and nut extracts. All these reactivities were inhibitable with the bromelain glycopeptide/ bovine serum albumin conjugate. Bee venom phospholipase and whole bee venom reacted weakly with YZ1/2.23 but more strongly with anti-horseradish peroxidase in a manner inhibitable with the bromelain glycopeptide/bovine serum albumin conjugate, while hemocyanin from Helix pomatia reacted poorly with YZ1/2.23 but did react with anti-horseradish peroxidase. It is concluded that the α1,3-fucose residue linked to the chitobiose core of plant glycoproteins is the most important residue in the epitope recognized by the two antibodies studied, but that the polyclonal anti-horseradish peroxidase antiserum also contains antibody populations that recognize the xylose linked to the core mannose of many plant and gastropod Nlinked oligosaccharides.

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Section: Introductionmentioning

confidence: 99%

Core 1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts

Wilson¹,

et al. 1998

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“…PLA 2 carries an N-glycan with ␣(1,3)-fucose but without ␤(1,2)-xylose (33). An earlier study by Kurosaka et al 1 The abbreviations used are: HRP, horseradish peroxidase; PLA 2 , phospholipase A 2 ; RAST, radioallergosorbent test; BRO, bromelain; PHA, phytohemagglutinin; PAGE, polyacrylamide gel electrophoresis; ConA, concanavalin A; PNGase, peptide N-glycosidase; HPAEC-PAD, high pH anion exchange chromatography coupled to pulsed amperometric detection; MALDI-TOF, matrix-assisted laser desorption ionizationtime of flight; 1 H NMR, proton nuclear magnetic resonance; BSA, bovine serum albumin; R S , Spearman rank correlation coefficient.…”

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confidence: 99%

“…Both these ␣(1,3)-fucose and ␤(1,2)-xylose are (at least partly) responsible for the immunogenicity of plant-glycoproteins in mammals (8,(27)(28)(29)(30). Horseradish peroxidase (HRP) 1 is a glycoprotein carrying N-glycans with both these monosaccharides (31). Polyclonal rabbit antiserum against HRP was shown to contain both anti-fucose and anti-xylose activity.…”

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confidence: 99%

β(1,2)-Xylose and α(1,3)-Fucose Residues Have a Strong Contribution in IgE Binding to Plant Glycoallergens

Ree¹,

Cabanes-Macheteau²,

Akkerdaas³

et al. 2000

Journal of Biological Chemistry

364

246

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Primary structures of the N-glycans of two major pollen allergens (Lol p 11 and Ole e 1) and a major peanut allergen (Ara h 1) were determined. Ole e 1 and Ara h 1 carried high mannose and complex N-glycans, whereas Lol p 11 carried only the complex. The complex structures all had a ␤(1,2)-xylose linked to the core mannose. Substitution of the proximal N-acetylglucosamine with an ␣(1,3)-fucose was observed on Lol p 11 and a minor fraction of Ole e 1 but not on Ara h 1. To elucidate the structural basis for IgE recognition of plant N-glycans, radioallergosorbent test analysis with protease digests of the three allergens and a panel of glycoproteins with known N-glycan structures was performed. It was demonstrated that both ␣(1,3)-fucose and ␤(1,2)-xylose are involved in IgE binding. Surprisingly, xylose-specific IgE antibodies that bound to Lol p 11 and bromelain did not recognize closely related xylose-containing structures on horseradish peroxidase, phytohemeagglutinin, Ole e 1, and Ara h 1. On Lol p 11 and bromelain, the core ␤-mannose is substituted with just an ␣(1,6)-mannose. On the other xylose-containing N-glycans, an additional ␣(1,3)-mannose is present. These observations indicate that IgE binding to xylose is sterically hampered by the presence of an ␣(1,3)-antenna.In the early 1980s, it was reported for the first time that IgE antibodies in sera of pollen allergic patients can be directed to carbohydrate determinants on glycoproteins (1-3). The carbohydrate nature of these epitopes was supported by several characteristic properties, such as their periodate sensitivity and their resistance to heating and protease digestion. IgE antibodies directed to these carbohydrate structures were shown to be extremely cross-reactive not only between different plant-derived glycoproteins but also to glycoproteins from invertebrate animals (e.g. seafood and insect venoms) (2, 4 -7).This high degree of cross-reactivity was explained by the conserved structure of N-glycans from plants and invertebrate animals, sharing several features that are not found in mammalian N-glycans (8). More recently, several research groups have confirmed the role of carbohydrate epitopes in IgE reactivity (9 -22).In plants, the N-glycosylation of proteins starts by the transfer of the oligosaccharide precursor Glc 3 Man 9 GlcNAc 2 in the endoplasmic reticulum (reviewed in Ref. 23). This structure can subsequently be modified by glycosidases and glycosyltransferases during transport of the glycoprotein through the endoplasmic reticulum, the Golgi apparatus, and the vacuole. Depending on the accessibility of the glycan side chain, these enzymes can convert the precursor to high mannose-type Nglycans ranging from Man 9 GlcNAc 2 to Man 5 GlcNAc 2 and then to complex-type N-glycans having an ␣(1,3)-fucose attached to the proximal glucosamine residue and/or a ␤(1,2)-xylose residue attached to the ␤-mannose. These linkages of fucose and xylose are typical for complex N-glycans from plants and invertebrate animals and are not found in mammals. Mo...

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“…The specificity of the RAST reaction for the var ious peaks was tested by performing the test with hu man sera with added protamine sulphate (1 mg/ml) as this has been shown to eliminate non-specific bind ing of IgE to allergen discs due to electrostatic inter actions [25], A slight reduction in the overall intensity of the reaction was noted, but this was spread over the whole focusing range. No individual peaks of activity were more affected than others (not shown).…”

Section: Preparative Isoelectric Focusing O F Incubation Productmentioning

confidence: 99%

Allergens of <i>Schistosoma mansoni</i>

Pierce¹,

Verwaerde²,

Damonneville³

et al. 1983

Int Arch Allergy Immunol

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The reaction of adult worm products of Schistosoma mansoni with IgE antibodies in infected human and Fischer rat sera has been studied using the Prausnitz-Küstner test and the radioallergosorbent test. Incubation of worms in water released most of the soluble material reacting with both rat and human sera in the radioallergosorbent test. Sera from infected Fischer rats recognized a fraction with pI 4.9–5.2 separated by preparative isoelectric focusing throughout the time course of infection, whereas human sera reacted with material focusing between pI 4.4 and 6.0. A peak of allergenic activity with an apparent molecular weight between 70,000 and 150J000 was obtained by gel filtration. Human bilharzian sera also reacted with material in the molecular weight range 12,000–25,000. Allergenic material bound specifically to concanavalin A-Sepharose, Lens culinaris agglutinin-Ultrogel, and wheat germ agglutinin-Ultrogel, but substantial allergenic activity was also present in unbound fractions.

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Cross-Reactions between Vegetable Foods, Pollen and Bee Venom Due to IgE Antibodies to a Ubiquitous Carbohydrate Determinant

Cited by 41 publications

References 1 publication

Core 1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts

Core 1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts

β(1,2)-Xylose and α(1,3)-Fucose Residues Have a Strong Contribution in IgE Binding to Plant Glycoallergens

Allergens of <i>Schistosoma mansoni</i>

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