Incomplete digestion of codfish represents a risk factor for anaphylaxis in patients with allergy

Untersmayr, Eva; Vestergaard, Helle; Malling, Hans‐Jørgen; Jensen, Louise Bjerremann; Platzer, Michael; Boltz‐Nitulescu, George; Scheiner, Otto; Skov, Per Stahl; Jensen‐Jarolim, Erika; Poulsen, Lars K.

doi:10.1016/j.jaci.2006.10.039

Cited by 88 publications

(82 citation statements)

References 41 publications

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“…Subsequently, we examined the digestibility of the whole fish protein extract compared with uncooked fish and determined the IgE-binding capacity of the resulting digestion fragments by IgE immunoblotting. IgE from fish allergic patients' sera could detect fragments after 15 min of gastric digestion of raw fish extract (data not shown), which is in accordance with a digestion study of raw cod protein extract, using a gastric tablet from Fédération International Pharmaceutique [15]. In contrast, cooked fish extract fragments were still recognized by patients' IgE after more than 120 min of digestion by pepsin (Fig.…”

Section: Discussionsupporting

confidence: 85%

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Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff

Griesmeier

Bublin

Radauer

et al. 2010

Molecular Nutrition Food Res

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Whiff (Lepidorhombus whiffiagonis) is a fish frequently consumed in Spain. Lep w 1, its major allergen, is a calcium-binding beta-parvalbumin. The resistance of Lep w 1 to heat denaturation and to digestion were studied by circular dichroism spectroscopy and by in vitro gastric digestion systems. Purified Lep w 1 was thermally stable up to 65 degrees C at neutral pH. Calcium depletion resulted in a change of its structure as determined by circular dichroism spectroscopy. A partial loss of structure was also observed at acidic pH; however, the allergen retained its full IgE-binding ability. The partially denatured Lep w 1 was easily digested by pepsin within 2 min. Further, the IgE reactivity of proteins extracted from cooked fish and their stability to proteolysis were analyzed. The extract revealed a higher number of IgE reactive bands than an extract from uncooked fish. IgE binding to these proteins could not be inhibited by an extract from uncooked fish. In contrast to a raw fish extract, the cooked extract showed higher resistance to pepsinolysis. The stability of Lep w 1 to thermal denaturation and digestion explains the high allergenicity of whiff.

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Section: Discussionsupporting

confidence: 85%

“…Untersmayer et al reported the pepsinolysis of raw codfish proteins to small fragments after incubation with simulated gastric fluid (SGF), pH 2 for 1 min [15].…”

Section: Introductionmentioning

confidence: 99%

Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff

Griesmeier

Bublin

Radauer

et al. 2010

Molecular Nutrition Food Res

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“…Some allergenic determinants in parvalbumin appear to be sequential, which may explain the low tendency for remission of fish allergy. Biologically active parvalbumin has been demonstrated in serum samples as early as 10 minutes after ingestion, peaking after one to two hours, suggesting some pre-gastric absorption (Untersmayr et al, 2007).…”

Section: Fish Muscle and Skinmentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

117

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Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

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“…The first fully characterized fish parvalbumin, Gad c 1 (previously named Allergen M) was isolated from Baltic cod (Gadus callarias, Aas and Elsayed, 1975;Elsayed and Apold, 1983). This sarcoplasmatic muscle protein is well-conserved, water-soluble, and resistant to heat, denaturing agents, and extreme pH (Bugajska-Schretter et al, 2000;Untersmayr et al, 2007). It has an isoelectic point (pI) of 4, and its tertiary structure contains three helix-loop-helix (EF hand) structural domains, with two high-affinity calcium ion-binding sites in the loop regions (Valenta et al, 1998).…”

Section: Fish Allergensmentioning

confidence: 99%

“…However, the major fish allergen parvalbumin from cod remained allergenic even after heating at 100 C, digestion with proteolytic enzymes, or chemical denaturation (Elsayed and Aas, 1971;Untersmayr et al, 2007). Bigeye tuna collagen was found to be very thermostable and to retain its allergenicity.…”

Section: Effects Of Food Processingmentioning

confidence: 99%

Fish Allergen Detection

Fæste

2009

Molecular Biological and Immunological Techniques and Applications for Food Chemists

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Incomplete digestion of codfish represents a risk factor for anaphylaxis in patients with allergy

Abstract: Hindered digestion puts patients with fish allergy at risk to develop severe allergic reactions at minute amounts of allergens.

Cited by 88 publications

References 41 publications

Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff

Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Fish Allergen Detection

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