Bee Venom PLA2 versus Snake Venom PLA2: Evaluation of Structural and Functional Properties

Abstract

Phospholipases A2 enzymes are found in many mammalian tissues and in animal venoms. Those present in bee venom (bvPLA2) and snake venom (svPLA2) have been studied more particularly for their biological activities of interest. Although they belong to the same family of secreted PLA2 (sPLA2), bvPLA2 and svPLA2 differ from a structural and functional point of view. In this review, we describe the morphological characteristics of these two enzymes and the structural determinants that govern their functions. After describing their cytotoxicity, we compared their biological activities, including antimicrobial, anti-tumor, anti-inflammatory, anti-neurodegenerative, and anti-nociceptive effects. In addition, we highlighted their therapeutical applications and deduced bvPLA2 has better potential than svPLA2 in biotechnological and pharmaceutical innovations.

Beehive Products as Antibacterial Agents: A Review

“…Melittin was twice as active as the crude BV against the tested bacteria (4 to 40 µg/mL). As for PLA 2 , it was only active against L. casei at >400 µg/mL [95,96]. Similarly, melittin showed antimicrobial activity against Staphylococcal strains as well as MRSA strains while PLA 2 did not show any effect on the same strains [97].…”

Advances in the Therapeutic Application of Small-Molecule Inhibitors and Repurposed Drugs against Snakebite

“…Nevertheless, the bioavailability of therapeutic compounds also plays an essential role in dose adjustment to treat a particular disease; therefore, final dose adjustment to treat snakebite envenomation is possible only after clinical trials. Unfortunately, however, the structural basis for the lower degree of potency (IC 50 value for 21 was 13.25 μM) of these inhibitors against bee venom sPLA 2 (positive control) compared to snake venom sPLA 2 sharing significant structural similarity 172 was not explained. Nonetheless, this study has kicked off the clinical use of 21 and 22 as field antidotes and antivenom adjuncts during snake envenomation.…”

Catalytically Active Snake Venom PLA2 Enzymes: An Overview of Its Elusive Mechanisms of Reaction

“…The svPLA 2 are small extracellular proteins with a molecular weight of 14–18 kDa, 120–135 amino acid residues, and 6–8 disulfide bridges that contribute to their high degree of stability and a pH optimum at 7. , In addition, these enzymes are characterized by a His48/Asp99 dyad at the active site with a Ca 2+ -binding loop and the requirement of mM Ca 2+ for catalytic activity. ,, Besides snake venom, secreted PLA 2 are found in scorpion and bee venom, among other animal venoms, and in several body fluids as nontoxic enzymes, including blood plasma, pancreatic secretions, seminal fluid, or tears. , svPLA 2 from elapid and viperid snakes share six disulfide bonds and an additional one in a different location on each …”