Details

Autor(en) / Beteiligte

• Blank, Simon
• Michel, Yvonne
• Seismann, Henning
• Plum, Melanie
• Greunke, Kerstin
• Grunwald, Thomas
• Bredehorst, Reinhard
• Ollert, Markus
• Braren, Ingke
• Spillner, Edzard

Titel

Evaluation of different glycoforms of honeybee venom major allergen phospholipase A2 (Api m 1) produced in insect cells

Ist Teil von

• Protein and peptide letters, 2011-04, Vol.18 (4), p.415-422

Ort / Verlag

Netherlands

Erscheinungsjahr

2011

Quelle

MEDLINE

Beschreibungen/Notizen

• Allergic reactions to hymenoptera stings are one of the major reasons for IgE-mediated anaphylaxis. However, proper diagnosis using venom extracts is severely affected by molecular cross-reactivity. In this study recombinant honeybee venom major allergen phospholipase A2 (Api m 1) was produced for the first time in insect cells. Using baculovirus infection of different insect cell lines allergen versions providing a varying degree of cross-reactive carbohydrate determinants as well as a non glycosylated variant could be obtained as secreted soluble proteins in high yields. The resulting molecules were analyzed for their glycosylation and proved to show advantageous properties regarding cross-reactivity in sIgE-based assays. Additionally, in contrast to the enzymatically active native protein the inactivated allergen did not induce IgE-independent effector cell activation. Thus, insect cell-derived recombinant Api m 1 with defined CCD phenotypes might provide further insights into hymenoptera venom IgE reactivities and contribute to an improved diagnosis of hymenoptera venom allergy.