Characterization of IgE Binding to Lupin, Peanut and Almond with Sera from Lupin-Allergic Patients

Holden, Lise; Sletten, Gaynour B. G.; Lindvik, Helene; Fæste, Christiane Kruse; Dooper, Maaike M.B.W.

doi:10.1159/000121461

Cited by 45 publications

(63 citation statements)

References 47 publications

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“…The sera from all fish-allergic patients and healthy controls were screened for IgE-binding activity as described elsewhere [26]. Briefly, ELISA plates were coated with 10 µg/ml fish extract/negative control (equine myoglobin; Sigma-Aldrich), or 40 µg/ml of fish hydrolysate.…”

Section: Methodsmentioning

confidence: 99%

“…Membranes were incubated overnight with individual patient sera (diluted 1:5–1:100), selected on the basis of IgE-binding activity in the indirect screening ELISA (hydrolysates incubated with serum pool, 1:20). Blots were further developed as described elsewhere [26]. Tris-buffered saline/0.05% Tween-20 containing 5% horse serum (Gibco, Paisley, UK) was used as blocking buffer, and the same buffer with 0.5 m M Ca 2+ was used as assay buffer.…”

Section: Methodsmentioning

confidence: 99%

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Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species

Sletten¹,

Do²,

Lindvik³

et al. 2009

Int Arch Allergy Immunol

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Background: Food-processing techniques may induce changes in fish protein immunogenicity. Allergens from >100 fish species have been identified, but little is known on the effects of processing on fish protein immunogenicity. Methods: IgE binding of sera of patients allergic to fresh and processed (smoked, salted/sugar-cured, canned, lye-treated and fermented) cod, haddock, salmon, trout, tuna, mackerel and herring and of hydrolysates based on salmon and whiting was investigated using immunoblot and inhibition ELISA. Results: Parvalbumin oligomers were identified using monoclonal and polyclonal antibodies. IgE binding was seen in most sera at 12–14 kDa (parvalbumin), and at 17–60 kDa for all fish except tuna. Changes in IgE binding appeared to reflect altered parvalbumin monomers and oligomers. Smoked haddock, salmon and mackerel had increased IgE binding and novel bands at 30 kDa. Chemically processed cod, salmon, trout and pickled herring had reduced or abolished IgE binding. The serum of 1 subject, however, had increased IgE binding to these products and also inhibition of binding by both fish hydrolysates to their constituent fish species. Conclusion: Process-induced changes in fish protein immunogenicity were more dependent on process rather than species, although individual responses varied. Changes in the allergenicity of a product may depend on the net effect of processing on parvalbumin oligomerization patterns, which may also vary in different species. Chemical processes generally caused loss in IgE-binding activity, though sensitization may occur to modified or degraded rather than intact peptides as shown by increased binding by chemically processed fish and hydrolysates in 1 subject. The clinical significance of these findings remains to be established.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species

Sletten¹,

Do²,

Lindvik³

et al. 2009

Int Arch Allergy Immunol

Self Cite

View full text Add to dashboard Cite

show abstract

“…The main lupin proteins able to bind IgE antibodies of allergic individuals are characterised by molecular weights in the range of 43-45 kDa [6,9,10]. However, similar effects may also be caused by other lupin proteins characterised by different molecular weight, i.e., 13 kDa [6], 29 kDa [11], 34 kDa [12], 38 kDa [8], and 66 kDa [13].…”

Section: Introductionmentioning

confidence: 99%

Immunoreactivity changes during lupin seed storage proteins digestion

Czubiński

Montowska

Springer

et al. 2017

Eur Food Res Technol

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“…Other potential allergens with MWs of 13, 29, 34, 38, and 66 kDa were isolated from lupin seeds by chromatographic methods and were studied for IgE-binding affinities Holden et al, 2008).…”

Section: Identified Allergensmentioning

confidence: 99%

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2014

EFSA Journal

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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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Characterization of IgE Binding to Lupin, Peanut and Almond with Sera from Lupin-Allergic Patients

Cited by 45 publications

References 47 publications

Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species

Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species

Immunoreactivity changes during lupin seed storage proteins digestion

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