Extract-Based and Molecular Diagnostics in Fish Allergy

Kuehn, Annette; Radauer, Christian; Lopata, Andreas L.; Kleine‐Tebbe, Jörg; Swoboda, Ines

doi:10.1007/978-3-319-42499-6_20

Cited by 6 publications

(16 citation statements)

References 46 publications

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“…Fish allergy is one of the 8 main food allergies and can affect both children and adults [1,2]. Labelling in industrialized countries requires mandatory declaration of fish content in food regardless of its quantity or proportion in which it is part of the final product.…”

Section: Epidemiologymentioning

confidence: 99%

“…The prevalence of occupational asthma due to fish allergen exposure is estimated to account for 2% to 8% of cases of occupational asthma among exposed individuals [1,5,6] and occurs mainly in countries where the fishing industry is important.…”

Section: Epidemiologymentioning

confidence: 99%

“…Of the 30 000 known species of fish, most are teleosts. A limited number of species are consumed frequently; these include Salmoniformes (salmon and trout), Gadiformes (cod and hake), Perciformes (mackerel and tuna), Clupeiformes (herring and sardine), Cypriniformes (carp and goldfish), Siluriformes (catfish), and Pleuronectiformes (sole, flounder, turbot, and halibut) [1,5,9,10].…”

Section: Biological Classificationmentioning

confidence: 99%

“…The parvalbumin protein is globular in shape and contains 6 helices (termed helices A-F). Parvalbumin is a member of the EF-hand calcium-binding protein family, which are characterized by the presence of a helix, a loop, and a second helix, with both helices arranged like the spread thumb and index finger of a human hand [1,4]. Calcium binds to these helices via ionic bonds, resulting in conformational stability.…”

Section: Parvalbuminmentioning

confidence: 99%

See 3 more Smart Citations

What Do We Know About Fish Allergy at the End of the Decade?

Kourani¹,

Corazza²,

Michel³

et al. 2019

J Investig Allergol Clin Immunol

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Fish allergy is one of the most common food allergies. It is usually considered to be IgE-mediated and correlates well with diagnostic tests such as prick tests and/or determination of specific IgE. Avoidance is the recommended treatment and is generally extended to all fish species. However, new clinical presentations have been described. These include non-IgE-mediated disease, monosensitization, and new syndromes that are sometimes associated, surprisingly, with cross-reactivity. Advances in molecular allergy have provided insights into new allergens and have increased our understanding of cross-reactivity. This paper focuses on recent publications providing information for clinicians involved in the management of fish allergy.

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Section: Epidemiologymentioning

confidence: 99%

Section: Epidemiologymentioning

confidence: 99%

Section: Biological Classificationmentioning

confidence: 99%

Section: Parvalbuminmentioning

confidence: 99%

See 2 more Smart Citations

What Do We Know About Fish Allergy at the End of the Decade?

Kourani¹,

Corazza²,

Michel³

et al. 2019

J Investig Allergol Clin Immunol

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show abstract

“…The tolerance of cartilaginous fish results from the absence of cross-reactivity of the basic α-lineage of the expressed PV 12 . In contrast, differences in the allergenic potency of bony fish species have been related to both the content and the pattern of the expressed β-PV isoforms 13,14,15 . However, the molecular signatures of and the relation between these features are still unknown.…”

Section: Introductionmentioning

confidence: 99%

Reconstruction of fish allergenicity from the content and structural traits of the component β-parvalbumin isoforms

Pérez-Tavarez

Carrera

Pedrosa

et al. 2019

Preprint

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Most fish-allergic patients have anti-β-parvalbumin (β-PV) immunoglobulin E (IgE), which cross-reacts among fish species with variable clinical effects. Although the β-PV load is considered a determinant for allergenicity, fish species express distinct β-PV isoforms with unknown pathogenic contributions. To identify the role various parameters play in allergenicity, we have taken Gadus morhua and Scomber japonicus models, determined their β-PV isoform composition and analyzed the interaction of the IgE from fish-allergic patient sera with these different conformations. We found that each fish species contains a major and a minor isoform, with the total PV content four times higher in Gadus morhua than in Scomber japonicus. The isoforms showing the best IgE recognition displayed protease-sensitive globular folds, and if forming amyloids, they were not immunoreactive. Of the isoforms displaying stable globular folds, one was not recognized by IgE under any of the conditions, and the other formed highly immunoreactive amyloids. The results showed that Gadus morhua muscles are equipped with an isoform combination and content that ensures the IgE recognition of all PV folds, whereas the allergenic load of Scomber japonicus is under the control of proteolysis. We conclude that the consideration of isoform properties and content may improve the explanation of fish species allergenicity differences.

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Allergenicity determination of Turbot parvalbumin for safety of fish allergy via dendritic cells, RBL‐2H3 cell and mouse model

Lin

et al. 2021

Eur Food Res Technol

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Extract-Based and Molecular Diagnostics in Fish Allergy

Cited by 6 publications

References 46 publications

What Do We Know About Fish Allergy at the End of the Decade?

What Do We Know About Fish Allergy at the End of the Decade?

Reconstruction of fish allergenicity from the content and structural traits of the component β-parvalbumin isoforms

Allergenicity determination of Turbot parvalbumin for safety of fish allergy via dendritic cells, RBL‐2H3 cell and mouse model

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