Allergic reactions to fish

O’Neil, Carol E.; Helbling, Arthur; Lehrer, Samuel B.

doi:10.1007/bf02914470

Cited by 79 publications

(4 citation statements)

References 56 publications

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“…It is worth noticing that fish are among the most common causes of food allergy mediated by IgE antibodies, especially in the countries where fish consumption is widespread. After ingestion of fish, some of the following clinical symptoms are rapidly induced in sensitized patients: urticaria, angioedema, respiratory symptoms (asthma and rhino conjunctivitis), gastrointestinal symptoms (diarrhea and vomiting), and, in severe cases, fatal anaphylaxis. , Extensive molecular studies have established that the major fish allergen is parvalbumin, a small calcium-binding protein, but also other fish proteins induce IgE-mediated allergy. − Reduced content in parvalbumin, found in sea fishes, may lead to a higher tolerance level to fish in sensible subject.…”

Section: Resultsmentioning

confidence: 99%

Monitoring Food Quality by Microfluidic Electrophoresis, Gas Chromatography, and Mass Spectrometry Techniques: Effects of Aquaculture on the Sea Bass (Dicentrarchus labrax)

Monti¹,

Napoli²,

Mainolfi³

et al. 2005

Anal. Chem.

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Monitoring food quality is a critical task for analytical chemistry and an important way to preserve human health. Fish is a valuable source of highly digestible proteins and contains large amounts of polyunsaturated fatty acids and fat-soluble vitamins. Since the world's wild fish stocks are limited, farmed fish is nowadays proposed as an alternative to consumers. It is now emerging that the fish muscle protein content is assuming great importance from an aquaculture perspective. Many data have been collected on the physiology and biochemistry of fish muscle, but few proteomic studies are available on farmed fish. Application of proteomics to aquaculture may play a key role in the development of new farming strategies. In this paper, a proteomic approach based on SDS-PAGE separation of proteins, in situ protein hydrolysis, de novo sequencing of peptides by MALDI and ESI MS(2), protein identification, and relative quantitation of protein by denaturing capillary electrophoresis was coupled with the determination of fatty acids and metal ions content by GM-MS and ICPMS in farmed and wild sea bass filet. Our results show that aquaculture could induce significant chemical and biochemical differences in fish muscle that may have an impact on food quality.

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Section: Resultsmentioning

confidence: 99%

Monitoring Food Quality by Microfluidic Electrophoresis, Gas Chromatography, and Mass Spectrometry Techniques: Effects of Aquaculture on the Sea Bass (Dicentrarchus labrax)

Monti¹,

Napoli²,

Mainolfi³

et al. 2005

Anal. Chem.

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“…1 Despite the enormous diversity of fish species, only a few orders of fish within the class Actinopterygii (ray-finned fish) are commonly consumed, namely, Salmoniformes, Perciformes, Gadiformes, Pleuronectiformes, Clupeiformes, and Cypriniformes. 2 Fish allergy limits the consumption of fish for some individuals. Fish is considered as a commonly allergenic food in the U. S., Europe, Canada, Australia, New Zealand, and elsewhere.…”

Section: ' Introductionmentioning

confidence: 99%

“…At least 27,000 species of fish have been scientifically described . Despite the enormous diversity of fish species, only a few orders of fish within the class Actinopterygii (ray-finned fish) are commonly consumed, namely, Salmoniformes, Perciformes, Gadiformes, Pleuronectiformes, Clupeiformes, and Cypriniformes . Fish allergy limits the consumption of fish for some individuals.…”

Section: Introductionmentioning

confidence: 99%

Evaluation and Comparison of the Species-Specificity of 3 Antiparvalbumin IgG Antibodies

Lee

Nordlee

Koppelman

et al. 2011

J. Agric. Food Chem.

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Parvalbumin is a pan-allergen in fish and frogs that triggers IgE-mediated reactions in fish-allergic individuals. Previous studies demonstrated that antibodies raised against fish and frog parvalbumins displayed varying specificity for different fish species, and thus, the applicability of these antibodies for potential use in immunoassays to detect fish residues were limited. We aimed to determine the specificity of 3 IgG antibodies for various fish species. Indirect enzyme-linked immunosorbent assay (ELISA) and IgG-immunoblotting were used to compare the reactivity of the polyclonal anticod parvalbumin antibody and the commercially available, monoclonal antifrog and monoclonal anticarp parvalbumin antibodies against raw muscle extracts of 29 fish species. All antibodies demonstrated varying specificities for different fish species. Of the 3 antibodies, the polyclonal anticod parvalbumin antibody is the most suitable for the detection of fish parvalbumins as it showed reactivity to the widest range of species, including herring, pilchard, carp, pike, cod, pollock, haddock, cusk, hake, bluegill, tilapia, bass, grouper, trout, catfish, and perch, although detection was still limited for several key fish species.

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“…The major fish allergen parvalbumin represents an extremely abundant allergen in many fish species, and the calcium-bound form has been shown to be remarkably stable. , Boiling and cooking fish can also lead to the formation of molecular aggregates and enhancement of IgE reactivity as shown for tuna, salmon, cod, flounder, and whiff. , Parvalbumin is usually found in the white muscle of fish where it is responsible for the relaxation of muscle fibers. The structure of the parvalbumin from carp was first determined by Kretsinger and Nockolds in 1973, which was the first EF-hand motif described .…”

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confidence: 99%

Pressure–Temperature Stability, Ca²⁺ Binding, and Pressure–Temperature Phase Diagram of Cod Parvalbumin: Gad m 1

et al. 2012

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Fish allergy is associated with IgE-mediated hypersensitivity reactions to parvalbumins, which are small calcium-binding muscle proteins and represent the major and sole allergens for 95% of fish-allergic patients. We performed Fourier transform infrared and tryptophan fluorescence spectroscopy to explore the pressure-temperature (p-T) phase diagram of cod parvalbumin (Gad m 1) and to elucidate possible new ways of pressure-temperature inactivation of this food allergen. Besides the secondary structure of the protein, the Ca(2+) binding to aspartic and glutamic acid residues was detected. The phase diagram was found to be quite complex, containing partially unfolded and molten globule states. The Ca(2+) ions were essential for the formation of the native structure. A molten globule conformation appears at 50 °C and atmospheric pressure, which converts into an unordered aggregated state at 75 °C. At >200 MPa, only heat unfolding, but no aggregation, was observed. A pressure of 500 MPa leads to a partially unfolded state at 27 °C. The complete pressure unfolding could only be reached at an elevated temperature (40 °C) and pressure (1.14 GPa). A strong correlation was found between Ca(2+) binding and the protein conformation. The partially unfolded state was reversibly refolded. The completely unfolded molecule, however, from which Ca(2+) was released, could not refold. The heat-unfolded protein was trapped either in the aggregated state or in the molten globule state without aggregation at elevated pressures. The heat-treated and the combined heat- and pressure-treated protein samples were tested with sera of allergic patients, but no change in allergenicity was found.

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Allergic reactions to fish

Cited by 79 publications

References 56 publications

Monitoring Food Quality by Microfluidic Electrophoresis, Gas Chromatography, and Mass Spectrometry Techniques: Effects of Aquaculture on the Sea Bass (Dicentrarchus labrax)

Monitoring Food Quality by Microfluidic Electrophoresis, Gas Chromatography, and Mass Spectrometry Techniques: Effects of Aquaculture on the Sea Bass (Dicentrarchus labrax)

Evaluation and Comparison of the Species-Specificity of 3 Antiparvalbumin IgG Antibodies

Pressure–Temperature Stability, Ca²⁺ Binding, and Pressure–Temperature Phase Diagram of Cod Parvalbumin: Gad m 1

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Allergic reactions to fish

Cited by 79 publications

References 56 publications

Monitoring Food Quality by Microfluidic Electrophoresis, Gas Chromatography, and Mass Spectrometry Techniques: Effects of Aquaculture on the Sea Bass (Dicentrarchus labrax)

Monitoring Food Quality by Microfluidic Electrophoresis, Gas Chromatography, and Mass Spectrometry Techniques: Effects of Aquaculture on the Sea Bass (Dicentrarchus labrax)

Evaluation and Comparison of the Species-Specificity of 3 Antiparvalbumin IgG Antibodies

Pressure–Temperature Stability, Ca2+ Binding, and Pressure–Temperature Phase Diagram of Cod Parvalbumin: Gad m 1

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Pressure–Temperature Stability, Ca²⁺ Binding, and Pressure–Temperature Phase Diagram of Cod Parvalbumin: Gad m 1