Glycans and glycan-specific IgE in clinical and molecular allergology: Sensitization, diagnostics, and clinical symptoms

Homann, Arne; Schramm, Gabriele; Jappe, Uta

doi:10.1016/j.jaci.2017.04.019

Cited by 55 publications

(61 citation statements)

References 124 publications

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“…This could be due to grass seeding strategies on paddocks, which is a hotly debated topic among horse owners. Natural (n) Cyn d 1, nPhl p 4, nApi g 5, nCup a 1 and MUXF3 on ISAC131, expresses cross‐reactive carbohydrate determinants (CCDs) which principally could lead to nonspecific IgE binding . However, only in one horse positive for Cyn d 1, simultaneous IgE reactivity could be detected to Phl p 4 and/or Phl p 1.…”

Section: Discussionmentioning

confidence: 99%

Molecular allergen profiling in horses by microarray reveals Fag e 2 from buckwheat as a frequent sensitizer

Einhorn

Hofstetter

Brandt

et al. 2018

Allergy

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BackgroundCompanion animals are also affected by IgE‐mediated allergies, but the eliciting molecules are largely unknown. We aimed at refining an allergen microarray to explore sensitization in horses and compare it to the human IgE reactivity profiles.MethodsCustom‐designed allergen microarray was produced on the basis of the ImmunoCAP ISAC technology containing 131 allergens. Sera from 51 horses derived from Europe or Japan were tested for specific IgE reactivity. The included horse patients were diagnosed for eczema due to insect bite hypersensitivity, chronic coughing, recurrent airway obstruction and urticaria or were clinically asymptomatic.ResultsHorses showed individual IgE‐binding patterns irrespective of their health status, indicating sensitization. In contrast to European and Japanese human sensitization patterns, frequently recognized allergens were Aln g 1 from alder and Cyn d 1 from Bermuda grass, likely due to specific respiratory exposure around paddocks and near the ground. The most prevalent allergen for 72.5% of the tested horses (37/51) was the 2S‐albumin Fag e 2 from buckwheat, which recently gained importance not only in human but also in horse diet.ConclusionIn line with the One Health concept, covering human health, animal health and environmental health, allergen microarrays provide novel information on the allergen sensitization patterns of the companion animals around us, which may form a basis for allergen‐specific preventive and therapeutic concepts.

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Section: Discussionmentioning

confidence: 99%

Molecular allergen profiling in horses by microarray reveals Fag e 2 from buckwheat as a frequent sensitizer

Einhorn

Hofstetter

Brandt

et al. 2018

Allergy

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“…There was no evidence of posttranslational glycosylation of eCry3.1Ab or mCry3A purified from MZIR098 maize leaf material or from the respective microbially produced proteins as shown by blot glycosylation assay. In general, there is a lack of consensus of the predictive value of considering the glycosylation status and any bearing on subsequent allergenicity of proteins (Altmann 2007;Garrido-Arandia et al 2014;Valenta et al 2015;Homann et al 2017). However, demonstrating that the microbially produced and plant-produced proteins are not differentially glycosylated (as was established for both eCry3.1Ab and mCry3A), can further support a conclusion that the two protein sources can be expected to display similar physicochemical properties.…”

Section: Discussionmentioning

confidence: 91%

Meeting technical challenges for protein characterization and surrogate equivalence studies that resulted from insecticidal protein co-expression in maize event MZIR098

2019

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Safety assessment of genetically modified plants includes protein characterization to confirm the intended trait protein expression. In addition, to conduct safety tests, the large amount of purified protein needed is usually met through the use of a surrogate, microbially produced protein source. Characterization of the eCry3.1Ab and mCry3A proteins as derived from Event MZIR098 maize was challenging because of the difficulty in purifying/isolating these proteins that are of similar molecular weight and have considerable shared sequence and immunogenicity. This also applies to establishing the biochemical equivalence to the microbially produced surrogate proteins, as highly-purified plant protein is required. While use of crude plant extracts facilitated functional equivalence testing with the surrogate proteins, a separate technical challenge had to be met. The eCry3.1Ab and mCry3A proteins display differentiated modes of action toward CRW pests, however, with the same overall target pest spectrum, no differential test organism existed to allow equivalence testing for one insecticidal protein in the presence of the other. To establish that the microbially produced proteins are suitable surrogates for the plant-produced proteins, the challenges in the protein purification and bioactivity testing had to be addressed. This article describes technical solutions to assess and characterize the insecticidal proteins in this new event and thereby confirm equivalence/suitability of the microbially produced protein surrogates. Keywords Insecticidal Á Cry protein Á Rootworm Á Transgenic Á Equivalence Á Peptide mass coverage Á Bioassay Abbreviations Bt Bacillus thuringiensis CPB Colorado potato beetle CRW Corn rootworm IRM Insect resistance management LC-MS/MS Liquid chromatography coupled to tandem mass spectroscopy PBST Phosphate buffered saline, pH 7.4 with 0.05% TweenÒ 20

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“…Glycomics of ticks provide interesting datasets on the potential effects of ticks on the host immune system. Identification of the N-glycan structures in the tick SGs revealed several CCDs associated with severe allergic reactions [30,31,45,46]. One of these is the fucose epitopes characteristic to insects.…”

Section: Cross-reactive Carbohydrate Determinants (Ccds) and Agal In mentioning

confidence: 99%

Alpha-Gal and Cross-Reactive Carbohydrate Determinants in the N-Glycans of Salivary Glands in the Lone Star Tick, Amblyomma americanum

et al. 2020

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Ticks are important ectoparasites and vectors of numerous human and animal pathogens. Ticks secrete saliva that contains various bioactive materials to evade the host defense system, and often facilitates the pathogen transmission. In addition, the Lone star tick saliva is thought to be the sensitizer in red meat allergy that is characterized by an allergic reaction to glycan moieties carrying terminal galactose-alpha-1,3-galactose (aGal). To assess N-glycome of Amblyomma americanum, we examined the N-glycan structures in male and female salivary glands at three different feeding stages and in carcasses of partially fed lone star ticks. We also surveyed the genes involved in the N-glycosylation in the tick species. The aGal epitopes and cross-reactive carbohydrate determinants (CCD) increases over time after the onset of blood feeding in both male and female A. americanum. These CCDs include xylosylation of the core mannose, 1,3-mono and 1,3- and 1,6-difucosylations of the basal GlcNac and mono- or diantennary aGal. Combinations of both xylosylation and aGal and fucosylation and aGal were also found on the N-glycan structures. While the enzymes required for the early steps of the N-glycosylation pathway are quite conserved, the enzymes involved in the later stages of N-glycan maturation in the Golgi apparatus are highly diverged from those of insects. Most of all, we propose that the aGal serves as a molecular mimicry of bioactive proteins during tick feedings on mammalian hosts, while it contributes as a sensitizer of allergy in atypical host human.

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Glycans and glycan-specific IgE in clinical and molecular allergology: Sensitization, diagnostics, and clinical symptoms

Cited by 55 publications

References 124 publications

Molecular allergen profiling in horses by microarray reveals Fag e 2 from buckwheat as a frequent sensitizer

Molecular allergen profiling in horses by microarray reveals Fag e 2 from buckwheat as a frequent sensitizer

Meeting technical challenges for protein characterization and surrogate equivalence studies that resulted from insecticidal protein co-expression in maize event MZIR098

Alpha-Gal and Cross-Reactive Carbohydrate Determinants in the N-Glycans of Salivary Glands in the Lone Star Tick, Amblyomma americanum

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