The effects of honey bee (Apis mellifera L.) venom and two of its constituents, melittin and phospholipase A2, on the cardiovascular system of the rat

A rabbit polyclonal antiserum raised against honey-bee (Apis mellifera) venom phospholipase A2 (PLA2) contains antibodies that react exclusively with its glycosylated variants and cross-react with plant glycoproteins. The interaction of anti-(horseradish peroxidase) antiserum with PLA2 suggests the existence of a carbohydrate determinant common to both glycoproteins. E.l.i.s.a. binding and inhibition experiments, employing glycoproteins and glycopeptides of plant and animal origin with known N-glycan structures, in combination with chemical and enzymic deglycosylation, identified alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine as the antigenic determinant. This fucose residue is present in the N-glycan of PLA2 and is frequently found in plant glycoproteins, whereas mammalian glycoproteins lack this modification.

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New approaches to old problems: Removal of phospholipase A2 results in highly active microsomal membranes from the honey bee, Apis mellifera

Pesticide Biochemistry and Physiology ◽

10.1016/j.pestbp.2019.04.014 ◽

2019 ◽

Vol 161 ◽

pp. 68-76

Author(s):

Marion Zaworra ◽

Ralf Nauen

Keyword(s):

Apis Mellifera ◽

Phospholipase A2 ◽

Honey Bee ◽

New Approaches ◽

Highly Active ◽

Microsomal Membranes

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Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities

Journal of Genetic Engineering and Biotechnology ◽

10.1186/s43141-020-00112-z ◽

2021 ◽

Vol 19 (1) ◽

Author(s):

Doaa A. Darwish ◽

Hassan M. M. Masoud ◽

Mohamed M. Abdel-Monsef ◽

Mohamed S. Helmy ◽

Hind A. Zidan ◽

...

Keyword(s):

Apis Mellifera ◽

Platelet Aggregation ◽

Phospholipase A2 ◽

Honey Bee ◽

Specific Activity ◽

Deae Cellulose ◽

High Specific Activity ◽

Inhibitory Effect ◽

Bee Venom ◽

Very High

Abstract Background Honey bee venom contains various enzymes with wide medical and pharmaceutical applications. Results The phospholipase A2 (PLA2) has been apparently purified from the venom of Egyptian honey bee (Apis mellifera lamarckii) 8.9-fold to a very high specific activity of 6033 U/mg protein using DEAE–cellulose and Sephacryl S-300 columns. The purified bee venom PLA2 is monomeric 16 kDa protein and has isoelectric point (pI) of 5.9. The optimal activity of bee venom PLA2 was attained at pH 8 and 45 °C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Conclusions The purified bee venom PLA2 exhibited anti-platelet aggregation and anti-coagulation activities which makes it promising agent for developing novel anti-clot formation drugs in future.

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