Three-dimensional model of the honeybee venom allergen Api m 7: structural and functional insights.

Dessislava Georgieva, Kerstin Greunke, Christian Betzel

Institute of Biochemistry and Molecular Biology, University of Hamburg, Laboratory of Structural Biology of Infection and Inflammation, c/o DESY, Notkestrasse 85, Building 22a, 22603 Hamburg, Germany.

Molecular bioSystems 2010 Jun

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Api m 7 is one of the major protease allergens of the honeybee venom. It consists of a serine protease-like (SPL) and a CUB domain. The knowledge about the structure and function of Api m 7 is limited mainly to its amino acid sequence. Three-dimensional models of the two structural domains were constructed using their amino acid sequences and the crystallographic coordinates of prophenoloxidase-activating factor (PPAF-II) as a template for the SPL domain and the coordinates of porcine spermadhesin PSP-II for the CUB domain. The structural organization of Api m 7 suggests that the CUB domain is involved in interactions with natural substrates while the SPL domain probably activates zymogens. IgE epitopes and antigenic sites were predicted. Api m 7 shows structural and functional similarity to the members of the PPAF-II family. Possible substrates, function and evolution of the enzyme are discussed in the paper.

Citation

Dessislava Georgieva, Kerstin Greunke, Christian Betzel. Three-dimensional model of the honeybee venom allergen Api m 7: structural and functional insights. Molecular bioSystems. 2010 Jun;6(6):1056-60