Allergens Api m 5 and Ves v 3 Molecular Weight Hymenoptera Venom

نویسندگان

  • Thomas Grunwald
  • Edzard Spillner
  • Johannes Ring
  • Reinhard Bredehorst
  • Markus W. Ollert
  • Liliana Cifuentes
  • Mareike McIntyre
  • Dana Rühl
  • Simon Blank
  • Henning Seismann
  • Benjamin Bockisch
  • Ingke Braren
چکیده

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منابع مشابه

Identification, recombinant expression, and characterization of the 100 kDa high molecular weight Hymenoptera venom allergens Api m 5 and Ves v 3.

Insect stings can cause life-threatening IgE-mediated anaphylactic reactions in venom-allergic patients. Although several compounds have already been described as venom allergens, prominent allergen candidates especially in the higher m.w. range have still remained elusive. Tandem mass spectrometry-based sequencing assigned a candidate gene to the most prominent putative high m.w. allergen Api ...

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

BACKGROUND Hymenoptera 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) fr...

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Vitellogenins Are New High Molecular Weight Components and Allergens (Api m 12 and Ves v 6) of Apis mellifera and Vespula vulgaris Venom

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 identif...

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تاریخ انتشار 2010