Cloning and characterization of profilin (Pru du 4), a cross-reactive almond (Prunus dulcis) allergen

Tawde, Pallavi; Venkatesh, Yeldur P.; Wang, Fang; Teuber, Suzanne S.; Sathe, Shridhar K.; Roux, Kenneth H.

doi:10.1016/j.jaci.2006.05.028

Cited by 59 publications

(54 citation statements)

References 59 publications

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“…pan-allergens). Based on immunoblotting and the strong inhibition of IgE binding to lupin by almond in the inhibition ELISA with serum from P4, a possible cross-reactivity could be expected between lupin α-conglutin and an almond protein approximately 14 kDa in size, for example 2S albumin or the profilin Pru du 4 [20, 24]. However, neither of these two almond proteins has, to our knowledge, been described to have homology to lupin α-conglutin.…”

Section: Discussionmentioning

confidence: 99%

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

Holden¹,

Sletten²,

Lindvik

et al. 2008

Int Arch Allergy Immunol

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Background: The increasing number of applications of sweet lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to lupin proteins. In particular, lupin allergy seems to appear in patients with an existing peanut allergy. In the present study, IgE-binding studies towards fractionated lupin seed proteins, and peanut and almond proteins were performed using sera from patients with confirmed lupin allergy. Methods:Immunoblotting and indirect ELISA were performed to investigate IgE binding to protein extracts. ELISA inhibition experiments were performed to investigate the presence of cross-reactive allergens in the protein extracts. Results: Immunoblotting and ELISA experiments demonstrated IgE binding to all lupin conglutins (α, β, γ and δ) as well as to peanut and almond proteins, with a unique IgE-binding profile for each patient. High IgE binding to α-conglutin was observed and IgE from the majority of patients similarly recognized two proteins within the α-conglutin-containing fraction, 40 and 43 kDa in size. Inhibition ELISA experiments showed that preincubation of sera with lupin conglutins, peanut and almond resulted in decreased IgE binding to lupin flour. Conclusions: Overall, these results indicate that α-, β-, γ- and δ-conglutins are candidate allergens in lupin and suggest a particularly strong allergenicity of α-conglutins. Furthermore, the results indicate the presence of cross-reactive allergens in lupin, peanut and almond.

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Section: Discussionmentioning

confidence: 99%

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

Holden¹,

Sletten²,

Lindvik

et al. 2008

Int Arch Allergy Immunol

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“…It is usually accumulated in the outer epidermal layers of plant organs and is thought to be responsible for the stronger allergenicity of the peels in comparison to the inner layers of almonds (Costa et al, 2012b). Pru du 4 has ≥ 90 % sequence identity with profilins from a variety of plant sources, including apple, cherry, peach, orange and melon, and is cross-reactive to ryegrass pollen profilins (Rodríguez-Perez et al, 2003;Tawde et al, 2006).…”

Section: Almondmentioning

confidence: 99%

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

Products¹

2014

EFS2

115

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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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“…In this case, the P. pastoris expression vector pPICZαA allowed expression of the recombinants as His-tagged fusion proteins. Although some studies suggest that use of native profilin from several plant sources makes for better diagnosis, at least in vitro, than the recombinant form [13,38], our study shows that the recombinant form of profilin may be very helpful in diagnosing sensitization to watermelon, even if the recombinant profilin is only a single isoform among many [39]. …”

Section: Discussionmentioning

confidence: 71%

Watermelon Profilin: Characterization of a Major Allergen as a Model for Plant-Derived Food Profilins

Cases

Pastor-Vargas²,

Gil-Dones³

et al. 2010

Int Arch Allergy Immunol

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Background: Plant profilins have been reported as minor allergens. They are a well-known pan-allergen family responsible for cross-reactivity between plant-derived foods and pollens. Watermelon profilin has been reported to be a major allergen in watermelon (Citrullus lanatus).The aim of this study was to characterize recombinant watermelon profilin, confirming its reactivity for diagnostic purposes and the development of immunotherapy. Methods: Native profilin was purified from watermelon extract by affinity chromatography using poly-L-proline. Recombinant His-tagged profilin was produced in Pichia pastoris yeast using pPICZαA vector and purified by metal chelate affinity chromatography. ELISA and immunoblot were carried out with sera from 17 watermelon-allergic patients. Biological activity was tested by the basophil activation test. Results: Native profilin and recombinant profilin were purified and identified by mass spectrometry. Both show similar IgE reactivity in vitro and are biologically active. Conclusions: Similarities were found in the IgE-binding patterns and biological activity of recombinant profilin and native profilin. Recombinant profilin may be a powerful tool for specific diagnosis.

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Cloning and characterization of profilin (Pru du 4), a cross-reactive almond (Prunus dulcis) allergen

Cited by 59 publications

References 59 publications

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

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

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

Watermelon Profilin: Characterization of a Major Allergen as a Model for Plant-Derived Food Profilins

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