The first reported case of Blaptica dubia cockroach allergy

Abstract Background Periplaneta americana and Blattella germanica cockroaches are widespread, and risk of sensitization increases in urban environments where these roaches thrive as household pests. There are no prior reports of Blaptica dubia cockroach allergy, though human exposure to B. dubia is increasing through commercial breeding as feeder insects. Case presentation A 50-year-old B. dubia cockroach breeder presented with progressively worsening upper and lower respiratory symptoms in recent years. Symptoms were worse with exposure to her B. dubia roach colony. Skin prick testing (SPT) to B. dubia cast skin, internal organs, and feces was performed in both the subject and a human control. Testing for P. americana and B. germanica sensitization was also performed in the subject. SDS–Polyacrylamide gel electrophoresis (PAGE), immunoblots, and enzyme-linked immunosorbent assays (ELISA) studies were performed using the subject and control serums to explore for specific IgE binding to B. dubia as well as P. americana. Our results showed SPT was positive to B. dubia internal organs in the subject and negative in the control. In the subject, SPT was negative to P. americana though intradermal (ID) testing was positive and serum specific IgE (sIgE) testing was negative to B. germanica. Immunoblotting of the subject's serum to B. dubia internal organ extract showed several distinct bands of IgE binding at 47 kilodaltons (kD), 68 kD, 74 kD, 83 kD, and 118 kD. The strongest band was at 118 kD on B. dubia immunoblotting, which was absent in P. americana on SDS-PAGE. ELISA studies showed an increased IgE response to both B. dubia and P. americana in the subject versus the control. Conclusions This case confirmed the first reported allergy to B. dubia cockroaches. There may be cross-reactivity between B. dubia and P. americana, though our case suggests SPT and sIgE testing using P. americana and B. germanica extract has potential to miss a B. dubia cockroach allergy. This allergy is likely underreported, and further study is needed to explore the natural history of B. dubia cockroach allergy.

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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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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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Oral allergy syndrome in children with pollen sensitization in Tomsk region

Rossiiskii Allergologicheskii ZHurnal ◽

10.36691/rja382 ◽

2016 ◽

Vol 13 (6) ◽

pp. 58-62

Author(s):

M M Fedotova ◽

O S Fedorova ◽

L M Ogorodova ◽

T A Evdokimova

Keyword(s):

Skin Prick Testing ◽

Clinical Stage ◽

Specific Ige ◽

Cross Sectional Study ◽

Cross Reactivity ◽

Oral Allergy Syndrome ◽

Pollen Allergens ◽

Cross Sectional ◽

Bet V 1 ◽

Tomsk Region

Background. Oral allergy syndrome (OAS) is defined as immediate IgE-mediated allergic reaction localized in the oral mucosa and developing after consuming raw fruits, vegetables, nuts, legumes in pollen sensitized patients. Objective. To study the prevalence of OAS in children in the Tomsk region. Material. The cross-sectional study in random groups of primary schoolchildren aged 7-10 years (n=13 010) from the Tomsk region, Russia, was performed in frames of (EuroPrevall, № FP6-2006-TTC-TU-5 Proposal 045879). During the screening phase a survey with standardized questionnaire was carried out. Clinical stage (n=1288) included clinical interviewing with parents/guardians, the clinical examination of patients, skin prick testing with extracts of food and pollen allergens (ALK-Abello, Spain), measurement of specific IgE level in serum to food and pollen allergens, component resolved diagnostics (ImmunoCAP, Phadia, Sweden). Results. OAS registered in 13,71% of children with pollen sensitization. The main triggers were apples, carrots, peaches, peanuts. Main cause of OAS in the Tomsk region was cross-reactivity to Bet v 1 - homologues belonging to PR-10 family: to apple - Mal d 1 (r=0,92; p=0,01); to peach - Pru p1 (r=0,87; p=0,01); to peanut - Ara h 8 (r=0,74; p=0,01); to hazelnut - Cor a 1 (r=0,76; p=0,01); to carrot - Dau c 1 (r=0,54; p=0,01). Conclusion. OAS was observed in 13,71% of children with pollen sensitization and was developesed due to crossreactivity to the birch allergen Bet v 1.

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Case Report: Allergic Reactivity to Mahaleb (Prunus mahaleb) Spice in a Subject With Almond and Other Tree Nut Allergies

Allergy & Rhinology ◽

10.1177/2152656720959083 ◽

2020 ◽

Vol 11 ◽

pp. 215265672095908

Author(s):

Lora Benoit ◽

Jongkit Masiri ◽

Harish Janagama ◽

Steven M. Gendel ◽

Mansour Samadpour

Keyword(s):

Skin Prick Testing ◽

Middle Eastern ◽

Specific Ige ◽

Cross Reactivity ◽

Enzyme Linked Immunosorbent Assay ◽

Tree Nut ◽

Polyclonal Igg ◽

History Of ◽

Specific Igg ◽

Food Recalls

Background Mahaleb is an aromatic spice prepared from the fruit stone of the St. Lucie Cherry that is used as a flavoring agent in traditional Turkish and Middle Eastern baking. Immunodiagnostic kits for almond, which are based on polyclonal almond-specific IgG antibodies, have been shown to demonstrate considerable cross-reactivity with mahaleb as was incidentally discovered during a cluster of allergen-related food recalls in 2015. Objective Though acute allergy to almond is somewhat common, allergies to mahaleb have not been previously documented. However, based on antigenic similarity observed with almond-specific IgG, it is predicted that mahaleb nut proteins would exhibit some level of cross-reactivity with almond-specific IgE and may therefore potentiate acute allergic symptoms in individuals with food allergy to almond. Case Presentation: Herein, we report on a 40-year old Caucasian female with longitudinal history of multiple tree nut allergies including allergy to almond, presenting with moderate pruritus and oropharyngeal swelling shortly following ingestion of mahaleb seed kernels. Methods and Results Skin-prick testing using extracts compounded from pistachio, almond, and mahaleb revealed positive wheals measuring 8, 3, and 7 mm respectfully. Indirect enzyme-linked immunosorbent assay (ELISA) using plate-bound antigens prepared from pistachio, almond, and mahaleb revealed IgG positive responses to all three targets. ELISA and Western blot analysis performed using goat anti-almond polyclonal IgG demonstrated significant cross-reactivity between almond and mahaleb, but not to pistachio. Conclusion This is the first documented case of acute allergy to mahaleb, co-occurring in the context of plural tree nut allergies, providing novel evidence that mahaleb may pose a risk to nut-allergic individuals and indicating a need for awareness of spice contamination with nut and mahaleb residues.

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

Clinical and Diagnostic Laboratory Immunology ◽

10.1128/cdli.10.2.229-232.2003 ◽

2003 ◽

Vol 10 (2) ◽

pp. 229-232 ◽

Cited By ~ 4

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.

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Contribution of conformational and linear IgE epitopes to ara H 2-specific IgE-binding - in vitro and in vivo studies

10.26226/morressier.5acdc65ed462b8029238dd5f ◽

2018 ◽

Author(s):

Angelika Tscheppe

Keyword(s):

Specific Ige ◽

In Vivo Studies ◽

Ara H 2 ◽

Ige Binding

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Food antigen-specific IgE in dogs with suspected food hypersensitivity

Tierärztliche Praxis Ausgabe K Kleintiere / Heimtiere ◽

10.1055/a-1274-9210 ◽

2020 ◽

Vol 48 (06) ◽

pp. 395-402

Author(s):

Sandra A. Baumann ◽

Cornelius Fritz ◽

Ralf S. Mueller

Keyword(s):

Clinical Relevance ◽

Specific Ige ◽

Elimination Diet ◽

Cross Reactivity ◽

Food Hypersensitivity ◽

Strong Correlations ◽

Odds Ratios ◽

Cross Reactions ◽

Ige Reactivity ◽

Food Specific Ige

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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