Biological activity of IgE specific for cross-reactive carbohydrate determinants

Foetisch, Kay; Westphal, Sandra; Lauer, Iris; Retzek, Mechthild; Altmann, Friedrich; Kolarich, Daniel; Scheurer, Stephan; Vieths, Stefan

doi:10.1067/mai.2003.173

Cited by 164 publications

(150 citation statements)

References 20 publications

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“…The clinical relevance of CCDspecific IgE is still a matter of debate but is deemed limited for the majority of patients (33). On the other hand, it was demonstrated that approximately one-third of the CCD-positive sera from patients with tomato allergy have biologically relevant CCD-specific IgE antibodies (34).…”

Section: Discussionmentioning

confidence: 99%

An antibody produced in tobacco expressing a hybrid β-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes

Bakker

Rouwendal

Karnoup

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

127

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N-glycosylation of a mAb may have a major impact on its therapeutic merits. Here, we demonstrate that expression of a hybrid enzyme (called xylGalT), consisting of the N-terminal domain of Arabidopsis thaliana xylosyltransferase and the catalytic domain of human ␤-1,4-galactosyltransferase I (GalT), in tobacco causes a sharp reduction of N-glycans with potentially immunogenic corebound xylose (Xyl) and fucose (Fuc) residues as shown by Western blot and MALDI-TOF MS analysis. A radioallergosorbent test inhibition assay with proteins purified from leaves of WT and these transgenic tobacco plants using sera from allergic patients suggests a significant reduction of potential immunogenicity of xylGalT proteins. A mAb purified from leaves of plants expressing xylGalT displayed an N-glycan profile that featured high levels of galactose, undetectable xylose, and a trace of fucose. Hence, a transgenic plant expressing the hybrid GalT might yield more effective and safer monoclonals for therapeutic purposes than WT plants and even transgenic plants expressing the unchanged GalT.biopharmaceutical ͉ glycosylation ͉ immunogenicity

show abstract

Section: Discussionmentioning

confidence: 99%

An antibody produced in tobacco expressing a hybrid β-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes

Bakker

Rouwendal

Karnoup

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

127

View full text Add to dashboard Cite

show abstract

“…e process leading to the clinical symptoms of aller gy can be re-enacted by test monitoring the degranulation of basophilic granulocytes either by measuring released histamine [10], interleukin 4 [11], or vesicle speci c protein markers [12]. Such histamine release tests were performed with tomato β-fructofuranosidase or albumin coupled CCDglyco peptides [10,11] and pointed at biological activity very similar to that of undoubted allergens such as Bet v 1. e obvious conclusion was that core α-1,3-fucosylated N-glycans are relevant allergenic epitopes causing clinical symptoms.…”

Section: Biological Signi Cance Of Plant/insect Ccdsmentioning

confidence: 99%

“…Such histamine release tests were performed with tomato β-fructofuranosidase or albumin coupled CCDglyco peptides [10,11] and pointed at biological activity very similar to that of undoubted allergens such as Bet v 1. e obvious conclusion was that core α-1,3-fucosylated N-glycans are relevant allergenic epitopes causing clinical symptoms.…”

Section: Biological Signi Cance Of Plant/insect Ccdsmentioning

confidence: 99%

Coping with cross-reactive carbohydrate determinants in allergy diagnosis

Altmann¹

2016

Allergo J

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“…Furthermore, the studies of glycosylation have mainly been focused on IgE or IgG binding and/or histamine release responses (22)(23)40). In the present study, the rFel d 1 ␤-chain was expressed with and without N-glycosylation (Table II, F-7/F-9).…”

Section: Discussionmentioning

confidence: 99%