scholarly journals Distinct Animal Food Allergens Form IgE-Binding Amyloids

Allergies ◽  
2020 ◽  
Vol 1 (1) ◽  
pp. 2
Author(s):  
Raquel Pérez-Tavarez ◽  
Milagros Castellanos ◽  
David Loli-Ausejo ◽  
María Pedrosa ◽  
José Luis Hurtado ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Allergic Patient ◽  
Full Length ◽  
Food Allergens ◽  
Native Structure ◽  
Animal Food ◽  
Ige Binding ◽  
D 12

Several animal food allergens assemble into amyloids under gastric-like environments. These aggregated structures provide Gad m 1 with an enhanced immunoglobulin E (IgE) interaction due to the fibrillation of the epitope regions. However, whether these properties are unique to Gad m 1 or shared by other food allergens has not yet been addressed. Using Bos d 5, Bos d 12 and Gal d 2 as allergen models and Gad m 1 as the control, aggregation reactions and the sera of milk, egg and fish allergic patients have been analyzed, assessing the IgE interactions of their amyloids. We found that amyloids formed by Bos d 12 and Gal d 2 full-length and truncated chains are recognized by the IgEs of milk and egg allergic patient sera. As with Gad m 1, in most cases amyloid recognition is higher than that of the native structure. Bos d 5 was not recognized under any fold by the IgE of the sera studied. These results suggest that the formation of IgE-binding amyloids could be a common feature to animal food allergens.

scholarly journals Animal Food Allergens Share the Formation of IgE-binding Amyloids

2020 ◽  
Author(s):  
Raquel Pérez-Tavarez ◽  
Milagros Castellanos ◽  
David Loli-Ausejo ◽  
María Pedrosa ◽  
José Luis Hurtado ◽  
...  
Keyword(s):  
Food Allergen ◽  
Allergic Patient ◽  
Full Length ◽  
Food Allergens ◽  
Animal Food ◽  
Ige Binding ◽  
Precursor Structure ◽  
D 12 ◽  
Amyloid Assembly

Several animal food allergens assembly into amyloids under gastric-like environments. These aggregated structures provide Gad m 1 with an enhanced IgE interaction due to the amyloid assembly of the epitope regions. However, whether these properties are unique of Gad m 1 or common to other food allergens has not yet been addressed. Using Bos d 5, Bos d 12 and Gal d 2 as food allergen models and Gad m 1 as control, aggregation reactions and the sera of milk, egg and fish allergic patients we have analyzed the IgE interaction of the distinct amyloids. We found that amyloids formed by Bos d 12 and Gal d 2 full-length and truncated chains are recognized by the IgEs of milk and egg allergic patient sera. As with Gad m 1, in most cases amyloid recognition is higher than that of the precursor structure. Bos d 5 was not recognized under any fold by the IgE of the sera studied. These results support that formation of IgE-binding amyloids might be a common feature to animal food allergen.

scholarly journals Detection of Cross-Reactivity for Atopic Immunoglobulin E against Multiple Allergens

2003 ◽  
Vol 10 (2) ◽  
pp. 229-232 ◽  
Author(s):  
Yee-Hsuan Chiou ◽  
Chung-Yee Yuo ◽  
Lin-Yu Wang ◽  
Shiao-ping Huang
Keyword(s):  
Immunoglobulin E ◽  
Competitive Inhibition ◽  
Allergic Patient ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Allergen Avoidance ◽  
Ige Binding ◽  
Specific Immunoglobulin E ◽  
Specific Immunoglobulin ◽  
The Common

ABSTRACT The existence of specific immunoglobulin E (IgE) allows us to determine the allergens that cause the allergic disease. For the purposes of allergen avoidance and immunotherapy, the measurement of specific IgE is widely applied in clinical laboratories. However, if IgE from the serum of an allergic patient exhibits reactivity to multiple allergens, it would cause a problem. The present study analyzes whether the serum IgE with multiple reactivity is due to the presence of unique IgE against the common epitope shared by different allergens or the presence of multiple IgEs against different epitopes on different allergens. The quantitative-competitive inhibition tests and the immunoblotting were applied to analyze the immunosimilarity among examined allergens. The result shows that the competitive inhibition of IgE binding between shrimp and crab allergens is higher than those between either shrimp and cockroach or between crab and cockroach. Furthermore, the results of immunoblotting are consistent with those of quantitative-competitive inhibition tests. These results allow us to detect the cross-reactivity for atopic IgE against multiple allergens.

Anaphylaxis and Emergency Treatment

PEDIATRICS ◽  
2003 ◽  
Vol 111 (Supplement_3) ◽  
pp. 1601-1608 ◽  
Author(s):  
Hugh A. Sampson
Keyword(s):  
Emergency Departments ◽  
Emergency Treatment ◽  
Immunoglobulin E ◽  
Antibody Therapy ◽  
The United States ◽  
Food Allergens ◽  
Tree Nuts ◽  
Immunomodulatory Therapies ◽  
Fish And Shellfish ◽  
Food Anaphylaxis

Food anaphylaxis is now the leading known cause of anaphylactic reactions treated in emergency departments in the United States. It is estimated that there are 30 000 anaphylactic reactions to foods treated in emergency departments and 150 to 200 deaths each year. Peanuts, tree nuts, fish, and shellfish account for most severe food anaphylactic reactions. Although clearly a form of immunoglobulin E-mediated hypersensitivity, the mechanistic details responsible for symptoms of food-induced anaphylaxis are not completely understood, and in some cases, symptoms are not seen unless the patient exercises within a few hours of the ingestion. At the present time, the mainstays of therapy include educating patients and their caregivers to strictly avoid food allergens, to recognize early symptoms of anaphylaxis, and to self-administer injectable epinephrine. However, clinical trials are now under way for the treatment of patients with peanut anaphylaxis using recombinant humanized anti-immunoglobulin E antibody therapy, and novel immunomodulatory therapies are being tested in animal models of peanut-induced anaphylaxis.

scholarly journals Detection and identification of allergens from Canadian mustard varieties of Sinapis alba and Brassica juncea

Biomolecules ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 489 ◽  
Author(s):  
L’Hocine ◽  
Pitre ◽  
Achouri
Keyword(s):  
Brassica Juncea ◽  
Protein Extraction ◽  
Immunoglobulin E ◽  
Sinapis Alba ◽  
Cross Reactivity ◽  
Protein Profiling ◽  
Ige Reactivity ◽  
Ige Binding ◽  
Reducing Conditions ◽  
Detection And Identification

Currently, information on the allergens profiles of different mustard varieties is rather scarce. Therefore, the objective of this study was to assess protein profiles and immunoglobulin E (IgE)-binding patterns of selected Canadian mustard varieties. Optimization of a non-denaturing protein extraction from the seeds of selected mustard varieties was first undertaken, and the various extracts were quantitatively and qualitatively analyzed by means of protein recovery determination and protein profiling. The IgE-binding patterns of selected mustard seeds extracts were assessed by immunoblotting using sera from mustard sensitized and allergic individuals. In addition to the known mustard allergens—Sin a 2 (11S globulins), Sin a 1, and Bra j 1 (2S albumins)—the presence of other new IgE-binding protein bands was revealed from both Sinapis alba and Brassica juncea varieties. Mass spectrometry (MS) analysis of the in-gel digested IgE-reactive bands identified the unknown ones as being oleosin, β-glucosidase, enolase, and glutathione-S transferase proteins. A bioinformatic comparison of the amino acid sequence of the new IgE-binding mustard proteins with those of know allergens revealed a number of strong homologies that are highly relevant for potential allergic cross-reactivity. Moreover, it was found that Sin a 1, Bra j 1, and cruciferin polypeptides exhibited a stronger IgE reactivity under non-reducing conditions in comparison to reducing conditions, demonstrating the recognition of conformational epitopes. These results further support the utilization of non-denaturing extraction and analysis conditions, as denaturing conditions may lead to failure in the detection of important immunoreactive epitopes.

scholarly journals GBS type III oligosaccharides containing a minimal protective epitope can be turned into effective vaccines by multivalent presentation

2019 ◽  
Author(s):  
F Carboni ◽  
F Angiolini ◽  
M Fabbrini ◽  
B Brogioni ◽  
A Corrado ◽  
...  
Keyword(s):  
Immune Responses ◽  
Group B Streptococcus ◽  
Full Length ◽  
Native Structure ◽  
Protective Response ◽  
Type Iii ◽  
Protective Epitope ◽  
Glycoconjugate Vaccines ◽  
Synthetic Oligosaccharides ◽  
Group B

Abstract Recent structural studies demonstrated that the epitope recognized by a monoclonal antibody representative of the protective response against the type III Group B Streptococcus polysaccharide was comprised within two of the repeating units that constitute the full-length native structure. Here we took advantage of this discovery to design a novel vaccine based on multivalent presentation of the identified minimal epitope on a carrier protein. We show that highly glycosylated short oligosaccharide conjugates elicit functional immune responses comparable to the full-length native polysaccharide. The obtained results pave the way to the design of well-defined glycoconjugate vaccines based on short synthetic oligosaccharides.

Relevance of IgE binding to short peptides for the allergenic activity of food allergens

2009 ◽  
Vol 124 (2) ◽  
pp. 328-336.e6 ◽  
Author(s):  
Melanie Albrecht ◽  
Yvonne Kühne ◽  
Barbara K. Ballmer-Weber ◽  
Wolf-Meinhard Becker ◽  
Thomas Holzhauser ◽  
...  
Keyword(s):  
Short Peptides ◽  
Food Allergens ◽  
Ige Binding ◽  
Allergenic Activity

scholarly journals Lateral electromigration and diffusion of Fc epsilon receptors on rat basophilic leukemia cells: effects of IgE binding.

1984 ◽  
Vol 99 (3) ◽  
pp. 778-787 ◽  
Author(s):  
M A McCloskey ◽  
Z Y Liu ◽  
M M Poo
Keyword(s):  
Cell Surface ◽  
Immunoglobulin E ◽  
Fc Receptors ◽  
Lateral Diffusion ◽  
Surface Proteins ◽  
Ige Binding ◽  
The Difference ◽  
D Values ◽  
Rbl Cells ◽  
Basophilic Leukemia

We have used in situ electromigration and post-field relaxation (Poo, M.-m., 1981, Annu. Rev. Biophys. Bioeng., 10:245-276) to assess the effect of immunoglobulin E (IgE) binding on the lateral mobility of IgE-Fc receptors in the plasmalemma of rat basophilic leukemia (RBL) cells. Bound IgE sharply increased the receptor's electrokinetic mobility, whereas removal of cell surface neuraminic acids cut it to near zero. In contrast, we found only a small difference between the lateral diffusion coefficients (D) of vacant and IgE-occupied Fc receptors (D: 4 vs. 3 X 10(-10) cm2/s at 24 degrees C). This is true for monomeric rat IgE; with mouse IgE, the difference in apparent diffusion rates was slightly greater (D: 4.5 vs. 2.3 X 10(-10) cm2/s at 24 degrees C). This range of D values is close to that found in previous photobleaching studies of the IgE-Fc epsilon receptor complex in RBL cells and rat mast cells. Moreover, enzymatic depletion of cell coat components did not measurably alter the diffusion rate of IgE-occupied receptors. Thus, binding of fluorescent macromolecular probes to cell surface proteins need not severely impede lateral diffusion of the probed species. If the glycocalyx of RBL cells does limit lateral diffusion of the Fc epsilon receptor, it must act primarily on the receptor itself, rather than on receptor-bound IgE.

scholarly journals Laboratory screening test with inhalant and food allergens in atopic Brazilian children and adolescents: a performance

2021 ◽  
Vol 49 (5) ◽  
pp. 42-48
Author(s):  
Ana Carolina Rozalem-Reali ◽  
Felipe Faria Pierotti ◽  
Aranda Carolina ◽  
Renata Rodrigues Cocco ◽  
Emanuel Cavalcanti Sarinho ◽  
...  
Keyword(s):  
Children And Adolescents ◽  
Immunoglobulin E ◽  
Allergic Sensitization ◽  
Screening Method ◽  
High Sensitivity ◽  
Allergic Diseases ◽  
Cross Sectional Study ◽  
Food Allergens ◽  
Cross Sectional ◽  
Brazilian Children

The Phadiatop Infant® (PhInf) is a panel developed to assess allergic sensitization (immunoglobulin E [IgE]) in children aged <5 years and combines inhalant and food allergens. The test has not been evaluated outside Europe. This is a cross-sectional study conducted at 11 pediatric allergy centers to evaluate PhInf as an allergic disease screening method in Brazilian children. Children as controls and patients (aged 6 months–18 years) were grouped according to their primary disease and age group. PhInf and specific serum IgE (sIgE) screening was performed for Dermatophagoides pteronyssinus (DP), cat and dog epithelia, a mix of grasses and pollens, eggs, cow’s milk, peanuts, and shrimp. Values ≥ 0.35 kUA/L (or PAU/L) were considered positive. A total of 470 children and adolescents, which included 385 patients and 85 controls, participated in the study (47.7% boys, average age: 6.3 years). In all, 72.6% of the participants had positive PhInf test (n = 341), with a higher proportion of those having food allergy (92.6%), atopic dermatitis (91.9%), and those aged >13 years having allergy (95%). The PhInf and sIgE agreement between patients (Kappa = 0.94, P < 0.001) and controls (Kappa = 0.84, P < 0.001) was high. PhInf and DP agreement in patients aged >13 years was excellent (Kappa = 0.936, P < 0.001). Compared with sIgE dosage, PhInf had high sensitivity (97%) and specificity (93%). Positivity of PhInf test in this population was high and had an excellent correlation with the allergens comprising the panel. It is a useful method for screening children suspected of having allergic diseases in a non-European country.

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