Reactivity of Shrimp Allergy-Related IgE Antibodies to Krill Tropomyosin

Nakano, Shigeru; Yoshinuma, Toshio; Yamada, Toshihiro

doi:10.1159/000109286

Cited by 30 publications

(14 citation statements)

References 43 publications

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“…The recombinant protein was subsequently produced and identified as a myosin light chain with high amino acid similarity to Bla g 8 from cockroaches. In addition, a sarcoplasmatic calcium-binding protein was identified as allergen in black tiger shrimp [25] and tropomyosin in two krill species [26] and an amphipod [27].…”

Section: Allergens In the Different Seafood Groupsmentioning

confidence: 99%

New insights into seafood allergy

Lopata

Lehrer

2009

Current Opinion in Allergy &Amp; Clinical Immunology

170

155

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Although cross-reactivity between crustacean and mollusks as well as mites is demonstrated, the often poor correlation of IgE reactivity and clinical symptoms calls for more detailed investigations. The recent development of hypoallergenic parvalbumin from carp could form the basis for safer vaccination products for treatment of fish allergy. Molecular characterization of more universal marker allergens for the three major seafood groups will improve current component-resolved clinical diagnosis and have a significant impact on the management of allergic patients, on food labeling and on future immunotherapy for seafood allergy.

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Section: Allergens In the Different Seafood Groupsmentioning

confidence: 99%

New insights into seafood allergy

Lopata

Lehrer

2009

Current Opinion in Allergy &Amp; Clinical Immunology

170

155

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“…Whole-shrimp extract was prepared essentially according to the methods reported in the literature with some modifications [20,21]. Whole shrimp bodies were blended for 3 min in 0.01 m (1:10 w/v) phosphate-buffered saline (PBS) and boiled for 15 min.…”

Section: Methodsmentioning

confidence: 99%

Structural and Immunological Characterization of Recombinant Pan b 1, a Major Allergen of Northern Shrimp, <b><i>Pandalus borealis</i></b>

Myrset

Barletta

Felice

et al. 2012

Int Arch Allergy Immunol

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Background: Shellfish allergy is one of the major causes of life-threatening allergic reactions to food. The shrimp species Pandalus borealis is the commercially most important coldwater shrimp species, and its protein extract is commonly used in shrimp allergy diagnostics. However, the DNA sequence of its major allergen, tropomyosin, designated Pan b 1, was not previously described. Our aim was to identify the cDNA sequence of Pan b 1 and to generate a recombinant protein with similar structure and allergenicity as the natural protein. Methods:P. borealis shrimps were caught in the Oslofjord (Norway). cDNA from Pan b 1 was generated, an N-terminal histidine tag was added, and the protein was expressed in Escherichia coli. The recombinant Pan b 1 was characterized by structural and IgE-binding studies and investigated further with basophil activation tests (BATs) and skin prick tests (SPTs) on Norwegian shrimp-allergic individuals. Results: The open reading frame encoded 284 amino acids that shared 97–100% identity with other shrimp tropomyosins. Mass spectroscopy of natural Pan b 1 confirmed the protein’s molecular mass and indicated the absence of posttranslational modifications. Circular dichroism spectroscopy revealed virtually identical spectra between recombinant and natural Pan b 1, which together with native PAGE and size exclusion chromatography results indicated a similar structure. Furthermore, immunoblot and ELISA studies as well as BATs and SPTs showed equivalent results of recombinant and natural Pan b 1. Conclusion: A recombinant tropomyosin from P. borealis was generated that can be used in diagnostics and further studies on tropomyosin allergenicity and specific immunotherapy.

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“…These tropomyosins show extensive IgE-binding cross-reactivity with shrimp, crab and lobster tropomyosins (Nakano et al, 2008). Krill tropomyosins and mantis shrimp tropomyosin have 82.3 to 89.8 % and > 90 % sequence identity with decapod tropomyosins, respectively (Motoyama et al, 2008).…”

Section: Non-decapod Crustaceansmentioning

confidence: 99%

Untitled

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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Reactivity of Shrimp Allergy-Related IgE Antibodies to Krill Tropomyosin

Cited by 30 publications

References 43 publications

New insights into seafood allergy

New insights into seafood allergy

Structural and Immunological Characterization of Recombinant Pan b 1, a Major Allergen of Northern Shrimp, <b><i>Pandalus borealis</i></b>

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