Characterization of allergenic food proteins for improved diagnostic methods

Beyer, Kirsten

doi:10.1097/00130832-200306000-00007

Cited by 32 publications

(16 citation statements)

References 79 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Characterization of new allergenic proteins could be effectively performed through recent advances in proteomics technology [17,25,37]. Thus, we used this approach to identify the allergenic proteins of local longtail tuna, T. tonggol .…”

Section: Discussionmentioning

confidence: 99%

“…The thermolabile properties of the bands were also successfully confirmed by the immunoblotting results of boiled extract of the fish. Initially, seafood allergens are often reported as heat-stable proteins and therefore resist the effect of cooking, processing or digestive processes [17]. However, other findings have confirmed the presence of thermolabile allergenic proteins in multiple species of fish [28,32,41], and canned tuna is considered the least-allergenic form of fish [33].…”

Section: Discussionmentioning

confidence: 99%

“…Most of these food allergens belong to parvalbumin, a calcium-binding sarcoplasmic protein with a molecular weight (MW) of about 12 kDa [5,6,8,16]. The first and best-identified parvalbumin allergen is Gad c 1 from codfish Gadus callarias which has high cross-reactivity between different fish species [6,17]. In subsequent molecular studies, parvalbumin has been identified as major allergen in multiple species of fish, such as salmon [18], Atlantic cod [19], carp [20,21], mackerel [22,23], Alaska pollack [24], blunt snout bream [25] and red stingray [26].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Identification of Parvalbumin and Two New Thermolabile Major Allergens of Thunnus tonggol Using a Proteomics Approach

Misnan

Murad²,

Meinir³

et al. 2013

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Background: The longtail tuna (Thunnus tonggol) is widely consumed in Asia. Parvalbumin, the main major allergen of fish, has been well identified in multiple fish species, yet little is known about the allergenic proteins in T. tonggol. Thus, the aim of this study was to characterize the major allergens of T. tonggol using a proteomics approach. Methods: Raw and boiled extracts of the fish were prepared. Fish proteins were separated by means of SDS-PAGE and two-dimensional (2-DE) electrophoresis. 1-DE immunoblotting of raw extract was performed with sera from fish-allergic patients. Ten sera were further analysed by 2-DE immunoblotting. Selected major allergenic protein spots were excised, trypsin digested and analysed by means of mass spectrometry. Results: SDS-PAGE of raw extract revealed 26 protein fractions, while boiled extract demonstrated fewer bands. The 2-DE gel profile of the raw extract further fractionated the protein bands to more than 100 distinct protein spots. 1-DE immunoblotting of raw extract exhibited two thermolabile protein fractions of 42 and 51 kDa as the major allergens, while the boiled extract only revealed a single IgE-binding band at 151 kDa. 2-DE immunoblotting of raw extract further detected numerous major IgE-reactive spots of 11-13, 42 and 51 kDa. Mass spectrometry analysis of the peptides generated from the 12, 42 and 51 kDa digested spots indicated that these spots were parvalbumin, creatine kinase and enolase, respectively. Conclusions: In addition to parvalbumin, two new thermolabile allergens were identified as major allergenic proteins of T. tonggol. This study proved that both thermostable and thermolabile proteins are important in local tuna allergy and should be included in diagnostic strategies.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of Parvalbumin and Two New Thermolabile Major Allergens of Thunnus tonggol Using a Proteomics Approach

Misnan

Murad²,

Meinir³

et al. 2013

Int Arch Allergy Immunol

View full text Add to dashboard Cite

show abstract

“…Protein microarrays have the ability to detect specific allergenic epitopes from individual food proteins and have revolutionized the management of food allergy [28]. Foodspecific IgE tests are limited by the fact that the foodspecific IgE levels fall in the in between range.…”

Section: Newer Diagnostic Methodsmentioning

confidence: 99%

“…In comparison, a prevalence rate of 2.5% in the random-digit dial tree nut and peanut questionnaire surveys in an unselected population in the US was reported. On a structural level, homologous proteins between peanuts and cashew nut, as well as peanut and hazelnut have been demonstrated [28]. Co-reactivity has also been reported between peanut and seeds like sesame, mustard, and poppy, and the peanut proteins Ara h 2, 6, and 7 has been shown to share sequence homology with seed storage proteins [15].…”

Section: Peanut Allergy and Tree Nut Allergiesmentioning

confidence: 99%

Food Allergy Overview in Children

Ramesh

2007

Clinic Rev Allerg Immunol

View full text Add to dashboard Cite

Food allergies have increased significantly in the past decade. An accurate history is crucial in approaching the management. At the outset, food intolerance must be distinguished from food allergies and, furthermore, these allergies should be classified into either an IgE, Non-IgE, or a mixed response. The clinical features vary from life-threatening anaphylaxis to milder IgE-mediated responses, atopic dermatitis, and gastrointestinal symptoms. The severity of the reaction and the potential risk for anaphylaxis on reexposure should be assessed. Milk, soy, egg, wheat, and peanut allergies are common in children, whereas peanut, tree nut, fish, shell fish allergies, and allergies to fruits and vegetables are common in adults. Structural proteins are important determinants of the severity of the reactions and may often predict the natural history and cross reactivity. Diagnostic work up must be guided by the clinical history. Skin testing and food-specific IgE done by standard methods are very useful, whereas oral challenges may be indicated in some situations. Majority of the patients outgrow their allergies to milk, soy, egg, and wheat, and some to peanut also, therefore, patients should be periodically reassessed. Novel diagnostic techniques which detect specific allergenic epitopes have been developed. Several newer therapies are promising.

show abstract

Food Allergy and Intolerance

Løvik

2009

General, Applied and Systems Toxicology

View full text Add to dashboard Cite

Food allergy is caused by immunologically mediated over‐reactivity against food components, and may be IgE mediated or non‐IgE mediated. The most serious form and the one of concern for regulatory authorities, is IgE‐mediated food allergy. Food intolerances often have unknown mechanisms. However, lactose intolerance and fructose intolerance are caused by known enzyme deficiencies, and gluten intolerance is caused by an autoimmune reaction elicited by gluten protein. IgE‐mediated food allergy often occurs together with skin allergy and respiratory allergy. The diagnosis of food allergy rests on three pillars: the case history, the demonstration of a specific IgE against the food in serum or by skin‐prick testing, and food challenge. Testing alone will grossly overestimate the presence of a clinically manifest food allergy. The diagnosis of food allergy is often difficult and resource‐demanding. Food allergy is most common in small children, but may be underestimated in young adults. There are geographical variations with regard to prevalence and which foods represent the most common allergens. Epidemiological data on food allergy are often uncertain. No validated animal models of food allergy exist. Prediction of allergenicity of a new protein depends on the overall weight of evidence derived from several sources, including comparison to known allergens in allergen databases.

show abstract

Characterization of allergenic food proteins for improved diagnostic methods

Abstract: The combination of food allergen characterization and protein or peptide microarray technology will enable us to develop improved diagnostic tools in food allergy.

Cited by 32 publications

References 79 publications

Identification of Parvalbumin and Two New Thermolabile Major Allergens of Thunnus tonggol Using a Proteomics Approach

Identification of Parvalbumin and Two New Thermolabile Major Allergens of Thunnus tonggol Using a Proteomics Approach

Food Allergy Overview in Children

Food Allergy and Intolerance

Contact Info

Product

Resources

About