A thermoactive secreted phospholipase A2 purified from the venom glands of Scorpio maurus: Relation between the kinetic properties and the hemolytic activity

• Published in: Toxicon (Oxford) 2013-09, Vol.72, p.133-142
• Main Authors: Louati, Hanen, Krayem, Najeh, Fendri, Ahmed, Aissa, Imen, Sellami, Mohamed, Bezzine, Sofiane, Gargouri, Youssef
• Format: Article
• Language: English
• Subjects: amino acid sequences; Amino acids; Analogies; Animals; Bridges (structures); calcium chloride; Chemical Fractionation; Chromatography, High Pressure Liquid; disulfide bonds; Erythrocytes; Erythrocytes - drug effects; hemolysis; Hemolytic activity; Hemolytic Agents - chemistry; Hemolytic Agents - isolation & purification; Hemolytic Agents - toxicity; Human; Humans; Hydrogen-Ion Concentration; Kinetics; molecular weight; Monolayers; phosphatidylcholines; Phospholipase; Phospholipase A2; phospholipases; Phospholipases A2 - chemistry; Phospholipases A2 - isolation & purification; Phospholipases A2 - toxicity; Phospholipids; Phospholipids monolayer; proteins; Rabbits; Rats; Scorpio maurus; Scorpion Venoms - enzymology; Scorpiones; Scorpions - chemistry; snakes; Surface pressure; Venom gland; venoms
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2013.06.017

A lipolytic activity was located in the scorpion venom glands (telsons), from which a phospholipase A2 (Sm-PLVG) was purified. Like known phospholipases A2 from scorpion venom, which are 14–18 kDa proteins, the purified Scorpio maurus-Phospholipase from Venom Glands (Sm-PLVG) has a molecular mass of 17 kDa containing long and short chains linked by disulfide bridge. It has a specific activity of 5500 U/mg measured at 47 °C and pH 8.5 using phosphatidylcholine as a substrate in presence of 8 mM NaTDC and 12 mM CaCl2. The NH2-terminal amino acid sequences of the purified Sm-PLVG showed similarities with those of long and short chains of some previously purified phospholipases from venom scorpions. Moreover, the Sm-PLVG exhibits hemolytic activity toward human, rabbit or rat erythrocytes. This hemolytic activity was related to its ability to interact with phospholipids’ monolayer at high surface pressure. These properties are similar to those of phospholipases isolated from snake venoms. •A thermoactive secreted phospholipase A2 purified from Tunisian Scorpio maurus venom glands (Sm-PLVG).•Sm-PLVG has a molecular mass of 17 kDa containing long and short chains linked by disulfide bridge.•S. maurus PLA2 exhibits direct hemolytic activity toward erythrocytes.•Hemolytic activity is related to interaction of Sm-PLVG with phospholipid monolayers at high surface pressure.