Pen a 1-specific IgE does not improve the accuracy of a shrimp allergy diagnosis among Japanese children due to cross-reactivity with Der p 10

Abstract Objective Knowledge of cross-reactions in food-sensitive dogs will influence the choice of elimination diets and the long-term management of those patients. The objective of this study was to evaluate food allergen-specific IgE tests of suspected allergic dogs for concurrent positive reactions as possible evidence for cross reactions between allergens. Material and methods Results of serum IgE tests from 760 suspected allergic dogs submitted to 2 laboratories were evaluated statistically. After the tested allergens were grouped by their phylogenetic relationship, odds ratios as well as a sensitivity analysis of the odds ratios were performed to evaluate if concurrent positive IgE results to 2 allergens occurred more often than expected. Results Within related allergen pairs 27% (laboratory 1) and 72% (laboratory 2) of the pairs could be considered as associated. For the unrelated allergen pairs only 6.8% and 10.6% of the analyzed pairs were considered associated respectively. Strong correlations were shown in the group of ruminant allergens, especially beef and lamb, and grain allergens. High rates of concurrent reactions were also detected in the poultry group, especially between chicken and duck, as well as between pork and ruminant allergens, and soy and grain allergens. Conclusion As our results showed not only correlations within related but also between non-related allergens, the possible relevance of carbohydrate moieties as well as panallergens for canine hypersensitivities warrants further study. Further investigations are necessary to distinguish co-sensitization from cross-reactions and determine the clinical relevance of food-specific IgE reactivity. Clinical relevance Due to possible cross reactivity related allergens, especially beef and lamb as well as grain allergens, should not be used for an elimination diet to avoid false results.

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Peanut-specific IgE antibodies in asymptomatic Ghanaian children possibly caused by carbohydrate determinant cross-reactivity

Journal of Allergy and Clinical Immunology ◽

10.1016/j.jaci.2013.04.023 ◽

2013 ◽

Vol 132 (3) ◽

pp. 639-647 ◽

Cited By ~ 57

Author(s):

Abena S. Amoah ◽

Benedicta B. Obeng ◽

Irene A. Larbi ◽

Serge A. Versteeg ◽

Yvonne Aryeetey ◽

...

Keyword(s):

Specific Ige ◽

Cross Reactivity ◽

Ige Antibodies ◽

Specific Ige Antibodies

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Specific IgE determination by RAST compared with skin and provocation tests in allergy diagnosis with birch pollen, timothy pollen and dog epithelium allergens

Clinical & Experimental Allergy ◽

10.1111/j.1365-2222.1974.tb01370.x ◽

1974 ◽

Vol 4 (2) ◽

pp. 131-140 ◽

Cited By ~ 43

Author(s):

S. AHLSTEDT ◽

N. ERIKSSON ◽

S. LINDGREN ◽

A. ROTH

Keyword(s):

Birch Pollen ◽

Specific Ige ◽

Allergy Diagnosis ◽

Provocation Tests ◽

Ige Determination

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Anaphylaxis following the consumption of pumpkin seeds in a two-year-old child tolerant to its pulp – a case study and a minireview

10.21203/rs.3.rs-112102/v1 ◽

2020 ◽

Author(s):

Julia Gawryjołek ◽

Hanna Ludwig ◽

Magdalena Żbikowska-Gotz ◽

Zbigniew Bartuzi ◽

Aneta Krogulska

Keyword(s):

Storage Proteins ◽

Sesame Seed ◽

Specific Ige ◽

Elimination Diet ◽

Cross Reactivity ◽

Amino Acid Sequences ◽

Pumpkin Seed ◽

Potential Health ◽

Prick Test ◽

Pumpkin Seeds

Abstract BackgroundPumpkin and its seeds are increasingly consumed by children for their potential health benefits. Each day, around 30% of teenagers consume nuts and seeds, including pumpkin seeds. However, there is some evidence that pumpkin seeds may exert allergenic effects and induce severe life-threatening anaphylaxis. Allergy for melon, cucumber, and zucchini, which belong to the same Cucurbitaceae family as pumpkin, are well known, opposite to pumpkin allergy. Few descriptions of allergic reactions associated with pumpkin have been published, especially in children. To date, three cases of pumpkin pulp and two seed cases have been reported among children. Our case report describes a case of pumpkin seed anaphylaxis in a child with good tolerance of pulp.Case presentationIn the present study, a two-year-old child experienced anaphylaxis: generalized urticaria, swollen lips and increasing dyspnea following the consumption of pumpkin seeds. The history showed that although the child had been receiving elimination diet because of atopic dermatitis, the basic dietary element was pumpkin pulp. The skin-prick test was positive for pumpkin seeds (5 mm) but negative for pumpkin pulp (1 mm); allergen-specific IgE was 1.34 kUA/L for seed, and 0.37 kUA/L for pulp. The component resolved diagnosis found IgE to sesame seed, buckwheat and walnut (storage proteins). Based on these findings, severe anaphylactic reaction to pumpkin seeds was identified.ConclusionsIt is possible to develop pumpkin seed anaphylaxis in a child with a tolerance to pumpkin pulp. Pumpkin seeds allergens have not been well characterized. Homology between the amino acid sequences in storage proteins may indicate cross reactivity between different edible seeds and nuts.

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Cross-Reactivity between IgE-Binding Proteins from Anisakis Simplex and Dermatophagoides Pteronyssinus

International Journal of Immunopathology and Pharmacology ◽

10.1177/039463200501800408 ◽

2005 ◽

Vol 18 (4) ◽

pp. 671-675 ◽

Cited By ~ 25

Author(s):

R. Bernardini ◽

G. Mistrello ◽

E. Novembre ◽

D. Roncarolo ◽

S. Zanotta ◽

...

Keyword(s):

Molecular Weight ◽

Binding Proteins ◽

Specific Ige ◽

Dermatophagoides Pteronyssinus ◽

Cross Reactivity ◽

Anisakis Simplex ◽

Cross Reaction ◽

Ige Binding ◽

Sds Page ◽

The Cross

An association was found between Anisakis simplex (As) and Dermatophagoides pteronyssinus (Dp) sensitization. One recent study shows a cross-reactivity between As and Dp and tropomyosin (tr) is suspected as being one of the proteins responsible of this cross-reaction. The aim of our study was: 1) to confirm the cross-reactivity between Dp and As; 2) to determine the importance of tr in this cross reaction. SDS-PAGE analysis of Dp and As (metabolic and somatic) extracts was carried out. Then an IgE immunoblotting test using serum from a patient who had specific IgE only to Dp and As and immunoblotting inhibition experiments using Dp extract and tr as inhibitors were performed. We found that patient's serum reacted: 1) against larval As antigens with a molecular weight (mw) of 25 kilodalton (kD) and a mw > 100 kD, 2) against various metabolic As antigens with a mw > 100 kD, a mw ranging approximately from 35 to 50 kD, and a mw around 20 kD, and 3) against Dp proteins with mw between 35 and 55 kD. Preincubation of patient's serum with Dp extract caused the disappearance of reactivity against antigens with a mw > 100 kD in both larval and metabolic As extracts and against proteins with mw ranging approximately from 35 to 50 kD in the metabolic As extract. Preincubation of patient's serum with As extract caused the disappearance of reactivity against antigens with mw between 35 and 55 kD in the Dp extract. Pre-incubation of patient's serum with tr did not induce any change in the immunoblotting profile. The results show that 1) cross-reactive components between Dp and As are some proteins with a mw ranging approximately from 35 to 50 kD and with a mw > 100 kD, and 2) tr is not involved in cross-reactivity between As and Dp.

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Sublingual Reactivity to rBET V1 and rPHL P1 in Patients with Oral Allergy Syndrome

International Journal of Immunopathology and Pharmacology ◽

10.1177/205873920601900114 ◽

2006 ◽

Vol 19 (1) ◽

pp. 205873920601900 ◽

Cited By ~ 8

Author(s):

F. Marcucci ◽

L. Sensi ◽

G. DI Cara ◽

G. Gidaro ◽

C. Incorvaia ◽

...

Keyword(s):

Specific Ige ◽

Cross Reactivity ◽

Oral Allergy Syndrome ◽

Control Group ◽

Recombinant Allergens ◽

Natural Extracts ◽

Target Organs ◽

High Concentrations

Oral Allergy Syndrome (OAS) in patients with pollen-induced rhinoconjunctivitis is caused by specific IgE recognizing cross-reacting epitopes of fruits and plants, which were clearly shown in vitro, but failed to be demonstrated in vivo by cross-challenges in the target organs. Considering the hypothesis of degradation of such epitopes in natural extracts, challenges with recombinant pollen allergens were done to evaluate the reactivity of the oral mucosa in OAS patients. Seventeen patients with OAS and rhinitis from birch (10) and grass pollen (7) and 10 non-atopic controls were studied by skin prick tests (SPT), allergen specific nasal challenges (ASNC) and allergen specific sublingual challenges (ASSC) with birch and timothy extracts and with rBet v1 and rPhl p1 at increasing concentrations from 1 to 1000 mcg/ml. None of the healthy subjects in the control group had any positive test for birch and timothy extracts or for recombinant allergens. In the OAS group the following results were observed: SPTs with recombinant allergens were positive in all patients, mostly at 10 mcg/ml concentration; ASNC with rBet v1 were positive in all patients, mostly at 100 mcg/ml; ASSC with natural pollen extracts were positive in only 2 of 17 patients, but in 15 of 17 with rBet v1 and rPhl p1, mostly at 500 mcg/ml and 1000 mcg/ml. ASSC with rBet v1 and rPhl p1 were positive with a mean concentration of 677 and 533 mcg/ml, respectively. The results of sublingual challenges with rBet v1 and rPhl p1 showed the in vivo cross-reactivity between pollens and foods in patients with OAS, but high concentrations of the recombinant allergens were needed to reproduce oral symptoms, thus explaining the failure of challenges performed with natural extracts, which have concentrations of major allergens lower than 50 mcg/ml. This indicates that sublingual mucosa is much less reactive to allergens than other surfaces, such as skin and nasal mucosa, probably because of its anatomic and immunologic peculiarity.

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Impact of Cross-reactivity between Major Peanut Allergens Ara h 2 and Ara h 6 on Specific IgE Measurements

Journal of Allergy and Clinical Immunology ◽

10.1016/j.jaci.2017.12.751 ◽

2018 ◽

Vol 141 (2) ◽

pp. AB237

Author(s):

Blanche Guillon ◽

Hervé Bernard ◽

Evelyne Paty ◽

Stephen C. Dreskin ◽

Karine Adel-Patient ◽

...

Keyword(s):

Specific Ige ◽

Cross Reactivity ◽

Ara H 2 ◽

Peanut Allergens ◽

Ara H 6

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Allergenic Characterization of Tropomyosin from the Dusky Brown Cockroach, Periplaneta fuliginosa

Clinical and Diagnostic Laboratory Immunology ◽

10.1128/cdli.11.4.680-685.2004 ◽

2004 ◽

Vol 11 (4) ◽

pp. 680-685 ◽

Cited By ~ 12

Author(s):

Kyoung Yong Jeong ◽

Heeyu Hwang ◽

Jongweon Lee ◽

In-Yong Lee ◽

Dong Soo Kim ◽

...

Keyword(s):

Recombinant Protein ◽

Periplaneta Americana ◽

Immunoglobulin E ◽

Expression System ◽

Specific Ige ◽

Cross Reactivity ◽

Enzyme Linked Immunosorbent Assay ◽

Inhibitor Concentration ◽

The Cross ◽

Elisa Inhibition

ABSTRACTHousehold arthropods are one of the most common causes of allergic diseases. Four species of cockroaches are found to reside in Korean homes, but published work deals almost exclusively with the German and American cockroaches. This study was undertaken to investigate the cross-reactive allergenic components of the dusky brown cockroach,Periplaneta fuliginosa. Enzyme-linked immunosorbent assay (ELISA) inhibition and immunoblot analyses for the dusky brown cockroach were performed withBlattella germanicaandDermatophagoides farinaeallergic sera. cDNA encoding tropomyosin, which is a well known cross-reactive pan-allergen, was cloned by reverse transcriptase PCR, and recombinant protein was produced by using a pET-28b expression system. Native tropomyosin was purified by ammonium sulfate fractionation and electroelution. The immunoglobulin E (IgE) reactivities of native and recombinant tropomyosins were compared by an ELISA inhibition study. All 30 sera tested showedP. fuliginosa-specific IgE, and the IgE-binding reactivity of theP. fuliginosaextract was inhibited as much as 79.4% by aB. germanicaextract and as much as 63.3% by aD. farinaeextract. The deduced amino acid sequence of cloned cDNA was identical with that ofPeriplaneta americanatropomyosin (98.5% nucleotide sequence identity). Seven of 26 (26.9%) allergic sera had IgE specific for recombinant protein, and the maximum inhibition ofP. fuliginosa-specific IgE achieved with recombinant tropomyosin was 37.7% at an inhibitor concentration of 10 μg/ml. Native tropomyosin inhibited the binding of IgE to theP. fuliginosa,B. germanica, andD. farinaeextracts by 65.0, 51.8, and 39% at an inhibitor concentration of 1 μg/ml.P. fuliginosaappears to possess allergens that are highly cross-reactive with allergens ofB. germanicaandD. farinae. Tropomyosin was found to be a major allergenic component accounting for the cross-reactivity between cockroaches and dust mites.

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Cephalosporins’ Cross-Reactivity and the High Degree of Required Knowledge. Case Report and Review of the Literature

Antibiotics ◽

10.3390/antibiotics9050209 ◽

2020 ◽

Vol 9 (5) ◽

pp. 209

Author(s):

Stefano D’Errico ◽

Paola Frati ◽

Martina Zanon ◽

Eleonora Valentinuz ◽

Federico Manetti ◽

...

Keyword(s):

Present Report ◽

Specific Ige ◽

Chain Structure ◽

Cross Reactivity ◽

Side Chain ◽

Mast Cell Tryptase ◽

Immunohistochemical Examination ◽

Femoral Blood ◽

The Subject ◽

High Degree

Antibiotic cross-reactivity represents a phenomenon of considerable interest as well as antibiotic resistance. Immediate reactions to cephalosporins are reported in the literature with a prevalence of only 1–3% of the population, while anaphylactic reactions are rarely described (approximately 0.0001–0.1%) as well as fatalities. Allergic reaction to cephalosporins may occur because of sensitization to unique cephalosporin haptens or to determinants shared with penicillins. Cross-reactivity between cephalosporins represents, in fact, a well-known threatening event involving cephalosporins with similar or identical R1- or R2-side chains. The present report describes the case of a 79-year-old man who suddenly died after intramuscular administration of ceftriaxone. Serum dosage of mast cell tryptase from a femoral blood sample at 3 and 24 h detected values of 87.7μg/L and 93.5μg/L, respectively (cut-off value 44.3 μg/L); the serum-specific IgE for penicillins, amoxicillin, cephaclor and also for the most common allergens were also determined. A complete post-mortem examination was performed, including gross, histological and immunohistochemical examination, with an anti-tryptase antibody. The cause of death was identified as anaphylactic shock: past administrations of cefepime sensitized the subject to cephalosporins and a fatal cross-reactivity of ceftriaxone with cefepime occurred due to the identical seven-position side chain structure in both molecules. The reported case offers food for thought regarding the study of cross-reactivity and the need to clarify the predictability and preventability of the phenomenon in fatal events.

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SPADE web service for prediction of allergen IgE epitopes

Nucleic Acids Research ◽

10.1093/nar/gkz331 ◽

2019 ◽

Vol 47 (W1) ◽

pp. W496-W501

Author(s):

Fabio Dall’Antonia ◽

Walter Keller

Keyword(s):

Binding Sites ◽

Specific Interaction ◽

Epitope Prediction ◽

Specific Ige ◽

Cross Reactivity ◽

Machine Learning Algorithms ◽

Training Data ◽

Third Party ◽

Prediction Methods ◽

Ige Binding

Abstract The specific interaction of allergens with IgE antibodies and the allergen mediated cross-linking of receptor-bound IgE are key events of allergic diseases. The elucidation of the IgE binding sites (the epitopes) on the allergen surface is an important goal of allergy research. Only few allergen-specific IgE epitopes have been determined experimentally to date. Epitope prediction methods represent a viable alternative to experimental methods and have worked well with linear epitopes. However, as most IgE epitopes are of conformational and/or discontinuous nature sequence based prediction methods have had limited success in these cases. Here, we present the web server of the program SPADE (https://spade.uni-graz.at), which is the server implementation of a previously published program (1). In this approach we utilize the structural homology of cross-reactive allergens combined with the immunological cross-reactivity data for the discrimination of putative IgE-binding sites from non-cross-reactive surface patches. The method, although predictive, does not rely on machine-learning algorithms and does not require training data. The SPADE server features an easy-to-use interface, an automated pipeline consisting of third-party, as well as own, newly developed routines and a comprehensive output page.

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