Molecular Cloning and Characterization of a Venom Phospholipase A2 from Apis mellifera spp

Honeybee venom plays a central role in the biodiversity and self-defense of honey bee, which protect them by allowing the stinger to immobilize, puncture and initiate allergy on their predators. Phospholipase A2 (PLA2) is one of the main allergic enzymes of honeybee venom, and it has been extensively studied in biochemical properties due to the toxicity to insects and other invaders causing hemolysis on erythrocytes. The present study described the results of cDNA cloning and chemical characterizations analysis of venom PLA2 from honeybee, Apis mellifera spp., an economically important insect for pollination on crops. The gene encoding Phospholipase A2 from honeybee (A. mellifera spp.) venom was isolated, cloned and its nucleotide sequence was determined. The nucleotide of PLA2 is 507 bp in length, and shared 99% and 96% homology with those of Apis mellifera ligustica and Apis cerana cerana, respectively. The amino acid sequence deduced of PLA2 resembled those of other bee subspecies, such as western honey bee (A. mellifera lingustica).