Human IgE Antibodies Against Cross-Reactive Carbohydrate Determinants

Hemmer, Wolfgang

doi:10.1007/978-3-7091-0870-3_8

Cited by 6 publications

(4 citation statements)

References 108 publications

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“…1 CCDs are ubiquitous in nature, being observed not only in helminths but also in insects, plants, and mammalians as components of their glycoproteins. 3 Not surprisingly, CCD structures identical or similar to those present in helminths can be observed in glycoproteins from diverse allergen sources, including pollen, mites, peanuts, and insect venoms. 3 Hence, even in the absence of worm infestations, more than 20% of allergic humans produce low-affinity, clinically irrelevant IgE responses to CCDs.…”

Section: Origins and Function Of Ige To Ubiquitous Cross-reactive Carmentioning

confidence: 97%

“…Because of their conservation, ubiquity, and capacity to be recognized by IgE antibodies, CCDs are among the broadest and most common causes of cross-reactivity among natural allergen sources and molecules. 3 Consequently, CCD-specific IgE plays a detrimental, confounding role in in vitro allergy diagnostics. Any allergen extract or native molecule containing CCD determinants will bind, in a rather nonspecific fashion, cross-reactive CCD-specific IgE antibodies whose inducer is often unknown.…”

Section: Ccd Cross-reactivity and Their Confounding Role In In Vitro mentioning

confidence: 99%

“…The presence of CCD in nPhl p 4 weakens the value of IgE testing to this molecule to identify grass pollen allergy, because these antibodies are very frequently induced by other allergen sources. 3 It is difficult to identify the allergen source that has induced CCD-specific antibodies. The recombinant, nonglycosylated Phl p 4 exhibits an approximately 10-fold higher potency in basophil release assays than the natural protein, showing that plant-derived CCDs may reduce the allergenicity of the natural allergen and dampen the immune response.…”

Section: Ccds Weaken Phl P 4 Relevancementioning

confidence: 99%

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IgE to cross-reactive carbohydrate determinants: Origins, functions, and confounding role in nPhl p 4-IgE assays

Matricardi

2020

Journal of Allergy and Clinical Immunology

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Section: Origins and Function Of Ige To Ubiquitous Cross-reactive Carmentioning

confidence: 97%

Section: Ccd Cross-reactivity and Their Confounding Role In In Vitro mentioning

confidence: 99%

Section: Ccds Weaken Phl P 4 Relevancementioning

confidence: 99%

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IgE to cross-reactive carbohydrate determinants: Origins, functions, and confounding role in nPhl p 4-IgE assays

Matricardi

2020

Journal of Allergy and Clinical Immunology

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“…Glycoproteins with these glyco-epitopes (known as Cross-reactive Carbohydrate Determinants, CCDs) [51], can elicit the production of antibodies in humans that, being specific for the carbohydrate target but not for the carrier proteins, can easily cross-react in in vitro allergy tests with non-homologous (but CCD-carrying) glycoproteins [27,51,52]. The actual contribution of CCDs to the allergenic potential of glycoproteins is an intricate and still controversial matter, and the clinical relevance of CCDs is highly debated [27,51,52,53]. Our identification of common CCDs in the major glycoforms of γ-conglutin could help in re-interpreting some of the conflicting data on the allergenic potential of this interesting bioactive glycoprotein.…”

Section: Discussionmentioning

confidence: 99%

In-Depth Glycoproteomic Characterization of γ-Conglutin by High-Resolution Accurate Mass Spectrometry

et al. 2013

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The molecular characterization of bioactive food components is necessary for understanding the mechanisms of their beneficial or detrimental effects on human health. This study focused on γ-conglutin, a well-known lupin seed N-glycoprotein with health-promoting properties and controversial allergenic potential. Given the importance of N-glycosylation for the functional and structural characteristics of proteins, we studied the purified protein by a mass spectrometry-based glycoproteomic approach able to identify the structure, micro-heterogeneity and attachment site of the bound N-glycan(s), and to provide extensive coverage of the protein sequence. The peptide/N-glycopeptide mixtures generated by enzymatic digestion (with or without N-deglycosylation) were analyzed by high-resolution accurate mass liquid chromatography–multi-stage mass spectrometry. The four main micro-heterogeneous variants of the single N-glycan bound to γ-conglutin were identified as Man2(Xyl) (Fuc) GlcNAc2, Man3(Xyl) (Fuc) GlcNAc2, GlcNAcMan3(Xyl) (Fuc) GlcNAc2 and GlcNAc 2Man3(Xyl) (Fuc) GlcNAc2. These carry both core β1,2-xylose and core α1-3-fucose (well known Cross-Reactive Carbohydrate Determinants), but corresponding fucose-free variants were also identified as minor components. The N-glycan was proven to reside on Asn131, one of the two potential N-glycosylation sites. The extensive coverage of the γ-conglutin amino acid sequence suggested three alternative N-termini of the small subunit, that were later confirmed by direct-infusion Orbitrap mass spectrometry analysis of the intact subunit.

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Microarray assessment of N-glycan-specific IgE and IgG profiles associated with Schistosoma mansoni infection in rural and urban Uganda

Nkurunungi

Diepen

Nassuuna

et al. 2019

Sci Rep

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Core β-1,2-xylose and α-1,3-fucose are antigenic motifs on schistosome N-glycans, as well as prominent IgE targets on some plant and insect glycoproteins. To map the association of schistosome infection with responses to these motifs, we assessed plasma IgE and IgG reactivity using microarray technology among Ugandans from rural Schistosoma mansoni ( Sm )-endemic islands (n = 209), and from proximate urban communities with lower Sm exposure (n = 62). IgE and IgG responses to core β-1,2-xylose and α-1,3-fucose modified N-glycans were higher in rural versus urban participants. Among rural participants, IgE and IgG to core β-1,2-xylose were positively associated with Sm infection and concentration peaks coincided with the infection intensity peak in early adolescence. Responses to core α-1,3-fucose were elevated regardless of Sm infection status and peaked before the infection peak. Among urban participants, Sm infection intensity was predominantly light and positively associated with responses to both motifs. Principal component and hierarchical cluster analysis reduced the data to a set of variables that captured core β-1,2-xylose- and α-1,3-fucose-specific responses, and confirmed associations with Sm and the rural environment. Responses to core β-1,2-xylose and α-1,3-fucose have distinctive relationships with Sm infection and intensity that should further be explored for associations with protective immunity, and cross-reactivity with other exposures.

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Human IgE Antibodies Against Cross-Reactive Carbohydrate Determinants

Cited by 6 publications

References 108 publications

IgE to cross-reactive carbohydrate determinants: Origins, functions, and confounding role in nPhl p 4-IgE assays

IgE to cross-reactive carbohydrate determinants: Origins, functions, and confounding role in nPhl p 4-IgE assays

In-Depth Glycoproteomic Characterization of γ-Conglutin by High-Resolution Accurate Mass Spectrometry

Microarray assessment of N-glycan-specific IgE and IgG profiles associated with Schistosoma mansoni infection in rural and urban Uganda

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