原创力文档recombinant phospholipase a1 (ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity重组磷脂酶a1(大v 1)从黄色夹克毒液改善膜翅目昆虫毒液过敏症的诊断.pdfVIP
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recombinant phospholipase a1 (ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity重组磷脂酶a1(大v 1)从黄色夹克毒液改善膜翅目昆虫毒液过敏症的诊断
Seismann et al. Clinical and Molecular Allergy 2010, 8:7
/content/8/1/7
CMA
R E S E A R C H Open Access
Research
Recombinant phospholipase A1 (Ves v 1) from
yellow jacket venom for improved diagnosis of
hymenoptera venom hypersensitivity
1 1 3 2 1 2
Henning Seismann , Simon Blank , Liliana Cifuentes , Ingke Braren , Reinhard Bredehorst , Thomas Grunwald ,
Markus Ollert*3 and Edzard Spillner* 1
Abstract
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) from yellow jacket venom (YJV) remained unavailable so
far.
Methods: Expression 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.
Results: Both 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
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