Kreuzreaktivität auf Bienen- und Wespengift

Hemmer, Wolfgang

doi:10.1007/s00105-008-1485-3

Cited by 15 publications

(7 citation statements)

References 28 publications

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“…Although there are several fundamental differences between the allergens in bee and wasp venom, 50 % or more of patients with HV‐AX show reactivity to both bee and wasp venom on serology. In these “double‐positive” patients, there can be independent sensitization to both venom types, a cross‐reaction to hyaluronidase in bee and wasp venom, or a reaction to cross‐reactive carbohydrate determinants (CCD) [11]. Hyaluronidase is present in both types of venom and is the main allergen containing CCD.…”

Section: Hymenoptera Venommentioning

confidence: 99%

Hymenoptera venom allergy

Przybilla

Ruëff

2010

J Deutsche Derma Gesell

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Allergic reactions to Hymenoptera stings usually present as large local reactions or systemic reactions with symptoms of immediate type allergy (anaphylaxis). In Central Europe they are predominantly elicited by stings of the honeybee or Vespula spp. Acute reactions are managed by symptomatic treatment. Long-term care includes patient education (allergen avoidance, course of action at re-sting) and prescription of an emergency kit for self-treatment. Venom immunotherapy is established as specific treatment for Hymenoptera venom allergic patients. Diagnosis of Hymenoptera venom anaphylaxis is based on history, skin tests and measurement of venom-specific serum IgE antibodies. "False negative" or "false positive" results are possible with all test methods. If standard tests are negative, additional tests using the patient's peripheral blood leucocytes can be useful. Venom immunotherapy is usually well tolerated. After reaching the maintenance dose, therapeutic efficacy should be assessed by a sting challenge test. If the patient again develops a systemic reaction, an increase of the maintenance dose (usually 200 microg are sufficient) nearly always induces protection. In most patients venom immunotherapy can be stopped after (3 to) 5 years. However, if there is an increased risk of sting anaphylaxis due to intense allergen exposure (e.g. in beekeepers) or if there are individual risk factors for particularly severe reactions (especially mastocytosis and/or elevated baseline serum tryptase concentration, severe cardiovascular disease), modifications of the standard venom immunotherapy are necessary.

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Section: Hymenoptera Venommentioning

confidence: 99%

Hymenoptera venom allergy

Przybilla

Ruëff

2010

J Deutsche Derma Gesell

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“…Thereby, the main problem arises from serologic double-positivity for A. mellifera and V. vulgaris venom of up to 50% of patients that have IgE against hymenoptera venoms [1]. Apart from true double-sensitisation this phenomenon is largely attributed to molecular cross-reactivity, either based on the presence of cross-reactive epitopes in homologues proteins of both venoms such as the hyaluronidases and dipeptidylpeptidases, or the presence of so-called cross-reactive carbohydrate determinants (CCD) which account for 70-80% of cross-reactive patients found within the double-positive cohort [2]. …”

Section: Introductionmentioning

confidence: 99%

Recombinant phospholipase A1 (Ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity

et al. 2010

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BackgroundHymenoptera venoms are known to cause life-threatening IgE-mediated anaphylactic reactions in allergic individuals. Proper diagnosis of hymenoptera venom allergy using venom extracts is severely affected by molecular cross-reactivities. Although non-glycosylated marker allergens would facilitate the identification of the culprit venom, the major allergen phospholipase A1 (Ves v 1) from yellow jacket venom (YJV) remained unavailable so far.MethodsExpression of Ves v 1 as wild type and enzymatically inactivated mutant and Ves v 5 in insect cells yielded soluble proteins that were purified via affinity chromatography. Functionality of the recombinant allergens was assessed by enzymatic and biophysical analyses as well as basophil activation tests. Diagnostic relevance was addressed by ELISA-based analyses of sera of YJV-sensitized patients.ResultsBoth major allergens Ves v 1 and Ves v 5 could be produced in insect cells in secreted soluble form. The recombinant proteins exhibited their particular biochemical and functional characteristics and were capable for activation of human basophils. Assessment of IgE reactivity of sera of YJV-sensitized and double-sensitized patients emphasised the relevance of Ves v 1 in hymenoptera venom allergy. In contrast to the use of singular molecules the combined use of both molecules enabled a reliable assignment of sensitisation to YJV for more than 90% of double-sensitised patients.ConclusionsThe recombinant availability of Ves v 1 from yellow jacket venom will contribute to a more detailed understanding of the molecular and allergological mechanisms of insect venoms and may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy.

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“…The presence of cross-reactive carbohydrates (CCD) in the allergens of Hymenoptera venoms is considered essential to serum antibody cross-reactivity that could be misinterpreted as multiple sensitizations hampering the correct diagnosis of the culprit insect in allergic patients [ 9 , 10 , 11 ]. This phenomenon could be observed in up to 59% of bee and wasp venoms allergic patients [ 19 , 26 ].…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, sera from sensitized patients may present multiple reactivities (30–50%) and cross-react with another Hymenoptera venom (60–70%) [ 7 , 8 ]. These reactions may occur due to several factors such as elevated specific IgE levels, independent of the sensitization to each venom; IgE antibodies with cross-reactivity against homologous proteins present in venoms or by the binding of IgE antibodies to cross-reactive carbohydrate determinants (CCD) [ 9 , 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity

Abram

Fernandes

Pérez-Riverol

et al. 2020

Toxins

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Allergic reactions to Hymenoptera venom, which could lead to systemic and even fatal symptoms, is characterized by hypersensitivity reactions mediated by specific IgE (sIgE) driven to venom allergens. Patients multisensitized to sIgE usually recognize more than one allergen in different Hymenoptera species. However, the presence of sIgE directed against Cross-Reactive Carbohydrate Determinant (CCD), which occurs in some allergens from Hymenoptera venom, hampers the identification of the culprit insects. CCD is also present in plants, pollen, fruits, but not in mammals. Bromelain (Brl) extracted from pineapples is a glycoprotein commonly used for reference to sIgE-CCD detection and analysis. In sera of fifty-one Hymenoptera allergic patients with specific IgE ≥ 1.0 KU/L, we assessed by immunoblotting the reactivity of sIgE to the major allergens of Apis mellifera, Polybia paulista and Solenopsis invicta venoms. We also distinguished, using sera adsorption procedures, the cases of CCD cross-reaction using Brl as a marker and inhibitor of CCD epitopes. The presence of reactivity for bromelain (24–28 kDa) was obtained in 43% of the patients, in which 64% presented reactivity for more than one Hymenoptera venom in radioallergosorbent (RAST) tests, and 90% showed reactivity in immunoblot analysis to the major allergens of Apis mellifera, Polybia paulista and Solenopsis invicta venoms. Sera adsorption procedures with Brl lead to a significant reduction in patients’ sera reactivity to the Hymenoptera allergens. Immunoblotting assay using pre- and post-Brl adsorption sera from wasp-allergic patients blotted with non-glycosylated recombinant antigens (rPoly p1, rPoly p5) from Polybia paulista wasp venom showed no change in reactivity pattern of sIgE that recognize allergen peptide epitopes. Our results, using Brl as a marker and CCD inhibitor to test sIgE reactivity, suggest that it could complement diagnostic methods and help to differentiate specific reactivity to allergens’ peptide epitopes from cross-reactivity caused by CCD, which is extremely useful in clinical practice.

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Kreuzreaktivität auf Bienen- und Wespengift

Cited by 15 publications

References 28 publications

Hymenoptera venom allergy

Hymenoptera venom allergy

Recombinant phospholipase A1 (Ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity

Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity

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