Abstract
Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom. However, no molecular information is currently available for acid phosphatases from A. cerana venom. In this study, an A. cerana venom acid phosphatase (AcVAP) was identified. The amino acid sequence analysis of the predicted AcVAP protein revealed high identity with other bee venom acid phosphatases. An anti-AcVAP antibody was produced against a recombinant AcVAP (46-kDa) expressed in in baculovirus-infected insect cells. Northern and Western blot analyses showed that AcVAP was expressed in the venom gland and was present as a 46-kDa protein in the secreted bee venom. The enzymatic properties of recombinant AcVAP were determined using p-nitrophenyl phosphate (p-NPP) as a substrate and exhibited the highest activity at pH4.8 and 45°C. Taken together, our data demonstrated that AcVAP functions as a bee venom acid phosphatase.
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