ArticlePloS one2013
Vitellogenins are new high molecular weight components and allergens (Api m 12 and Ves v 6) of Apis mellifera and Vespula vulgaris venom.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 86 citations in OpenAlex.
- The Venom Revolution in Biomedicine: Unlocking Nature's Toxin Toolkit for Therapeutic Innovation.Toxicology reports · 2026Review
- Immunogenic and cross-reactive carbohydrate determinants in ticks and other arthropods.Journal of applied biomedicine · 2026Review
- Homology Analysis ofToxins · 2026Article
- The Clinical Importance of Component-Based Diagnostic Test in Patients Planned for Venom Immunotherapy.International archives of allergy and immunology · 2026Article
- The green lacewing venom system and the complex mechanisms underlying its evolution.Molecular biology and evolution · 2026Article
- In vitro diagnostics in hymenoptera venom allergy: Current concepts and perspectives.Allergologie select · 2026Review
- ExploringHeliyon · 2024Article
- Unusual functions of insect vitellogenins: minireview.Physiological research · 2023Review
- Component-Resolved Evaluation of the Risk and Success of Immunotherapy in Bee Venom Allergic Patients.Journal of clinical medicine · 2022Article
- Intracutaneous Skin Tests and Serum IgE Levels Cannot Predict the Grade of Anaphylaxis in Patients with Insect Venom Allergies.Journal of asthma and allergy · 2022Article
- Cross-reactivity between tick and wasp venom can contribute to frequent wasp sensitization in patients with the α-Gal syndrome.Clinical and translational allergy · 2022Article
- A Review of Honeybee Venom Allergens and Allergenicity.International journal of molecular sciences · 2021Review
- An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.Scientific reports · 2021Article
- Characterization of Venom Components and Their Phylogenetic Properties in Some Aculeate Bumblebees and Wasps.Toxins · 2020Article
- IgE and T Cell Reactivity to a Comprehensive Panel of Cockroach Allergens in Relation to Disease.Frontiers in immunology · 2020Article
- Immunology of Bee Venom.Clinical reviews in allergy & immunology · 2018Review
- Allergen-specific immunotherapy of Hymenoptera venom allergy - also a matter of diagnosis.Human vaccines & immunotherapeutics · 2017Review
- Component resolved diagnostics for hymenoptera venom allergy.Current opinion in allergy and clinical immunology · 2017Review
- Component Resolved Diagnosis in Hymenoptera Anaphylaxis.Current allergy and asthma reports · 2017Review
- Diagnostics in Hymenoptera venom allergy: current concepts and developments with special focus on molecular allergy diagnostics.Allergo journal international · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND/
objectivesAnaphylaxis due to hymenoptera stings is one of the most severe clinical outcomes of IgE-mediated hypersensitivity reactions. Although allergic reactions to hymenoptera stings are often considered as a general model for the underlying principles of allergic disease, venom immunotherapy is still hampered by severe systemic side effects and incomplete protection. The identification and detailed characterization of all allergens of hymenoptera venoms might result in an improvement in this field and promote the detailed understanding of the allergological mechanism. Our aim was the identification and detailed immunochemical and allergological characterization of the low abundant IgE-reactive 200 kDa proteins of Apis mellifera and Vespula vulgaris venom. METHODS/PRINCIPAL
findingsTandem mass spectrometry-based sequencing of a 200 kDa venom protein yielded peptides that could be assigned to honeybee vitellogenin. The coding regions of the honeybee protein as well as of the homologue from yellow jacket venom were cloned from venom gland cDNA. The newly identified 200 kDa proteins share a sequence identity on protein level of 40% and belong to the family of vitellogenins, present in all oviparous animals, and are the first vitellogenins identified as components of venom. Both vitellogenins could be recombinantly produced as soluble proteins in insect cells and assessed for their specific IgE reactivity. The particular vitellogenins were recognized by approximately 40% of sera of venom-allergic patients even in the absence of cross-reactive carbohydrate determinants.
conclusionWith the vitellogenins of Apis mellifera and Vespula vulgaris venom a new homologous pair of venom allergens was identified and becomes available for future applications. Due to their allergenic properties the honeybee and the yellow jacket venom vitellogenin were designated as allergens Api m 12 and Ves v 6, respectively.
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