Vitellogenins are new high molecular weight components and allergens (Api m 12 and Ves v 6) of Apis mellifera and Vespula vulgaris venom

PLoS One. 2013 Apr 23;8(4):e62009. doi: 10.1371/journal.pone.0062009. Print 2013.

Abstract

Background/objectives: Anaphylaxis 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 findings: Tandem 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.

Conclusion: With 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.

MeSH terms

  • Allergens / chemistry
  • Allergens / genetics
  • Allergens / immunology*
  • Amino Acid Sequence
  • Animals
  • Bee Venoms / chemistry
  • Bee Venoms / immunology*
  • Bees / chemistry
  • Cloning, Molecular
  • Desensitization, Immunologic / methods
  • Humans
  • Hypersensitivity, Immediate / immunology*
  • Immunoglobulin E / blood
  • Immunoglobulin E / immunology*
  • Insect Bites and Stings / immunology*
  • Insect Proteins / chemistry
  • Insect Proteins / genetics
  • Insect Proteins / immunology*
  • Molecular Sequence Data
  • Molecular Weight
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sf9 Cells
  • Vitellogenins / chemistry
  • Vitellogenins / genetics
  • Vitellogenins / immunology*
  • Wasp Venoms / chemistry
  • Wasp Venoms / immunology*
  • Wasps / chemistry

Substances

  • Allergens
  • Api m 12 allergen, Apis mellifera
  • Bee Venoms
  • Insect Proteins
  • Recombinant Proteins
  • Ves v 6 allergen, Vespula vulgaris
  • Vitellogenins
  • Wasp Venoms
  • Immunoglobulin E

Grants and funding

The authors have no support or funding to report.