Expression levels of parvalbumins determine allergenicity of fish species

Griesmeier, Ulrike; Vázquez-Cortés, Sonia; Bublin, Merima; Radauer, Christian; Ma, Yan; Briza, Peter; Fernández‐Rivas, Montserrat; Breiteneder, Heimo

doi:10.1111/j.1398-9995.2009.02162.x

Cited by 111 publications

(64 citation statements)

References 30 publications

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“…Crossreactivity among different fish species occurs frequently because of the high amino acid sequence identity of β-parvalbumins (frequently reported as allergenic) from different fish species [4]. This means that most people with an allergy to one fish species are advised to avoid all fish species.…”

Section: Introductionmentioning

confidence: 99%

Novel approach for the simultaneous detection of DNA from different fish species based on a nuclear target: quantification potential

2012

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The development of DNA-based methods for the identification and quantification of fish in food and feed samples is frequently focused on a specific fish species and/or on the detection of mitochondrial DNA of fish origin. However, a quantitative method for the most common fish species used by the food and feed industry is needed for official control purposes, and such a method should rely on the use of a single-copy nuclear DNA target owing to its more stable copy number in different tissues. In this article, we report on the development of a real-time PCR method based on the use of a nuclear gene as a target for the simultaneous detection of fish DNA from different species and on the evaluation of its quantification potential. The method was tested in 22 different fish species, including those most commonly used by the food and feed industry, and in negative control samples, which included 15 animal species and nine feed ingredients. The results show that the method reported here complies with the requirements concerning specificity and with the criteria required for real-time PCR methods with high sensitivity.

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Section: Introductionmentioning

confidence: 99%

Novel approach for the simultaneous detection of DNA from different fish species based on a nuclear target: quantification potential

2012

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“…Allergenomic studies in seafood products have been only sparingly applied using SDS-PAGE and immunoblotting [105] or these techniques combined with MS [106,107]. Other scientists investigated the allergenic mechanisms of the parvalbumin fraction with myofibrillar protein fraction using crystallography [108] or immunological tools [109] which are not proteomic techniques in sensu stricto [110].…”

Section: Allergen Detectionmentioning

confidence: 99%

“…In seafood products, the major fish allergens are parvalbumins beta (ß-PRVBs), a calcium-binding protein with low molecular weight (~10-12 KDa), with acidic pI, present in high amounts in the sarcoplasmic fraction of white muscles of fish and resistant to heat and digestive enzymes [104,105].…”

Section: Allergen Detectionmentioning

confidence: 99%

High-Throughput Proteomics: A New Tool for Quality and Safety in Fishery Products

Tedesco¹,

Mullen²,

Cristóbal

2014

CPPS

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Abstract:In order to cope with the increasing demand for fishery products, sensitive technological tools are required to ensure high quality and wholesomeness and to monitor their production process in a sustainable manner while complying with the strict standards imposed by regulatory authorities. Proteomics may assist the industry as it allows an unbiased approach in the discovery of biomarkers that could be used to increase our understanding of different biological, physiological and ecological aspects that may be advantageous in optimizing quality and safety in aquatic species. The aim of this review is to highlight the potential of cost-effective high-throughput technologies, such as those offered by proteomics using "on-line" mass spectrometry to improve the efficiency of the industry in identifying biomarkers relevant for safe high quality products.

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“…Parvalbumin has been reported to play a very dominant role, with the majority of fish-allergic patients being sensitized mainly to this allergen in a broad spectrum of fish species [2,9,10]. The first parvalbumin identified and characterized as an allergen was the major codfish allergen, Gad c 1 [11,12].…”

Section: Introductionmentioning

confidence: 99%

Development of a Hypoallergenic Recombinant Parvalbumin for First-in-Man Subcutaneous Immunotherapy of Fish Allergy

Zuidmeer-Jongejan

Huber

Swoboda

et al. 2015

Int Arch Allergy Immunol

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Background: The FAST (food allergy-specific immunotherapy) project aims at developing safe and effective subcutaneous immunotherapy for fish allergy, using recombinant hypoallergenic carp parvalbumin, Cyp c 1. Objectives: Preclinical characterization and good manufacturing practice (GMP) production of mutant Cyp (mCyp) c 1. Methods:Escherichia coli-produced mCyp c 1 was purified using standard chromatographic techniques. Physicochemical properties were investigated by gel electrophoresis, size exclusion chromatography, circular dichroism spectroscopy, reverse-phase high-performance liquid chromatography and mass spectrometry. Allergenicity was assessed by ImmunoCAP inhibition and basophil histamine release assay, immunogenicity by immunization of laboratory animals and stimulation of patients' peripheral blood mononuclear cells (PBMCs). Reference molecules were purified wild-type Cyp c 1 (natural and/or recombinant). GMP-compliant alum-adsorbed mCyp c 1 was tested for acute toxicity in mice and rabbits and for repeated-dose toxicity in mice. Accelerated and real-time protocols were used to evaluate stability of mCyp c 1 as drug substance and drug product. Results: Purified mCyp c 1 behaves as a folded and stable molecule. Using sera of 26 double-blind placebo-controlled food-challenge-proven fish-allergic patients, reduction in allergenic activity ranged from 10- to 5,000-fold (1,000-fold on average), but with retained immunogenicity (immunization in mice/rabbits) and potency to stimulate human PBMCs. Toxicity studies revealed no toxic effects and real-time stability studies on the Al(OH)₃-adsorbed drug product demonstrated at least 20 months of stability. Conclusion: The GMP drug product developed for treatment of fish allergy has the characteristics targeted for in FAST: i.e. hypoallergenicity with retained immunogenicity. These results have warranted first-in-man immunotherapy studies to evaluate the safety of this innovative vaccine.

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Expression levels of parvalbumins determine allergenicity of fish species

Abstract: The parvalbumins of cod, whiff and swordfish are highly cross-reactive. The high amino acid sequence identity among cod, whiff and swordfish parvalbumins results in the observed IgE cross-reactivity. The low allergenicity of swordfish is due to the low expression levels of its parvalbumin.

Cited by 111 publications

References 30 publications

Novel approach for the simultaneous detection of DNA from different fish species based on a nuclear target: quantification potential

Novel approach for the simultaneous detection of DNA from different fish species based on a nuclear target: quantification potential

High-Throughput Proteomics: A New Tool for Quality and Safety in Fishery Products

Development of a Hypoallergenic Recombinant Parvalbumin for First-in-Man Subcutaneous Immunotherapy of Fish Allergy

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