Role of carbohydrate moieties in cross‐reactivity between different components of <i>Parietaria Judaica</i> pollen extract

Mucci, N.; Liberatore, P; Federico, Rodolfo; Forlani, Fabio; Felice, Gabriella Di; Afferni, Claudia; Tinghino, Raffaella; Cesare, Fabrizio De; Pini, Carlo

doi:10.1111/j.1398-9995.1992.tb02083.x

Cited by 23 publications

(16 citation statements)

References 36 publications

(9 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Others thought that it was impossible to have carbohydrate-specific IgE antibodies because carbohydrate determinants were supposed to be T cell independent. Several groups have confirmed the existence of IgE antibodies against N-glycans on glycoproteins from plants and invertebrate animals since they were first reported [3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27]. Immunologically, antibody responses to these structures can best be compared to the classical concept of haptens.…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Ree¹

2002

Int Arch Allergy Immunol

173

119

View full text Add to dashboard Cite

Allergenicity of plant and invertebrate N-glycans has been shown to be caused by the presence of two typical nonmammalian substitutions: an α(1,3)-fucose linked to the proximal N-acetylglucosamine and a β(1,2)-xylose linked to the core mannose. IgE antibodies against these carbohydrate structures are induced upon exposure to pollen or after insect stings, and result in extensive cross-reactivity to plant and invertebrate foods. These cross-reactive IgE antibodies have been shown to possess variable degrees of biological activity, but have never been convincingly shown to induce clinical food allergy. The most likely explanation for this lack of clinical relevance has to be sought in a combination of epitope valency and antibody affinity. In diagnostic tests, these antibodies are at the basis of many false-positive test results for food allergy. Recombinant technologies offer the possibility to produce allergens that do not carry IgE-binding glycans. Whether their absence or presence is of importance for the application of recombinant allergens in immunotherapy is still largely unknown.

show abstract

Section: Introductionmentioning

confidence: 99%

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Ree¹

2002

Int Arch Allergy Immunol

173

119

View full text Add to dashboard Cite

show abstract

“…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. That caution should be applied to interpreting results of chemical deglycosylation with trifluoromethanesulfonic acid is borne out by the finding that the circular dichroism spectrum of Ole e I reveals complete loss of the native conformation of the protein (Batanero et al, 1994).…”

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

View full text Add to dashboard Cite

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.

show abstract

“…Many allergenic proteins in vegetable foods, insects and pollens are glycoproteins with N-linked glycan moieties, which are associated with their immunoreactivities [3, 4, 5, 6, 7, 8, 9, 10, 11]. The oligosaccharide moiety of phospholipase A 2 was reported to be an IgE determinant site of a major allergen from honeybee venom [12].…”

Section: Introductionmentioning

confidence: 99%

Occurrence of IgE Antibody-Recognizing N-Linked Glycan Moiety of a Soybean Allergen, Gly m Bd 28K

Hiemori

Bando²,

Ogawa³

et al. 2000

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Background: It has been reported that N-linked glycan moieties of glycoproteins function as IgE-reactive determinants. Gly m Bd 28K, a soybean allergen, was a glycoprotein with glycan moieties, which are supposed to be the Man₃GlcNAc₂ backbone with the β1→2 xylose and α1→3 fucose branches. The purpose of the present study was to examine the IgE-binding ability of the glycan moiety of Gly m Bd 28K in the binding reaction with patients’ sera. Methods: A peptide containing the glycan moiety was prepared from Gly m Bd 28K by digestion with lysyl endopeptidase. The binding site of the glycan moiety was determined by amino acid sequence analyses. The glycan moiety of the allergen was characterized using anti-horseradish peroxidase antibody (anti-HRP) recognizing the N-linked glycan moieties of glycoproteins. The binding of patients’ IgE antibodies with their glycan moiety was examined by an immunostaining technique using the glycopeptide and its deglycosylated peptide derived from Gly m Bd 28K. Results: The binding site of the glycan moiety in Gly m Bd 28K was shown to be its Asn20 residue. Gly m Bd 28K did react with anti-HRP and the sera of soybean-sensitive patients, but the binding of IgE antibodies was inhibited by the preincubation with anti-HRP. Moreover, the glycopeptide also reacted with the sera of soybean-sensitive patients, but its deglycosylated peptide did not react with any IgE antibodies of patients’ sera. Conclusions: The specific IgE antibodies recognizing the N-linked glycan moieties of Gly m Bd 28K and other glycoproteins with homologous glycan moieties occur in the sera of soybean-sensitive patients. It was indicated that the N-linked glycan moieties such as that of Gly m Bd 28K may be one of the common IgE-reactive determinants distributed in various plant food proteins.

show abstract

Role of carbohydrate moieties in cross‐reactivity between different components of Parietaria Judaica pollen extract

Cited by 23 publications

References 36 publications

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

Carbohydrate Epitopes and Their Relevance for the Diagnosis and Treatment of Allergic Diseases

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

Occurrence of IgE Antibody-Recognizing N-Linked Glycan Moiety of a Soybean Allergen, Gly m Bd 28K

Contact Info

Product

Resources

About