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<p>The venom of scorpions contains a diverse array of bioactive compounds, including mucoproteins, nucleotides, and enzymes. Among these, phospholipase A<sub>2</sub> (PLA<sub>2</sub>) plays a critical role in hydrolyzing plasma membrane phospholipids, leading to the release of fatty acids and lysophospholipids. In this study, characterized Maurolipin was selected as a candidate for recombinant protein production and evaluation of its anti-leishmanial activity. The recombinant protein was expressed in <i>Escherichia coli</i> strain Origami (DE3) and purified using a Ni-NTA resin column. The anti-parasitic activity of Maurolipin was tested against <i>Leishmania major</i> promastigotes, the causative agent of zoonotic cutaneous leishmaniasis (ZCL). The growth inhibitory effect was assessed across a range of concentrations (40 to 0.07 μg/ml). Leishmanicidal activity was determined by propidium iodide (PI) staining and flow cytometry, while cytotoxicity to RAW 264.7 macrophages was evaluated using an MTT assay. Maurolipin exhibited potent anti-leishmanial effects, with a 24-hour growth inhibition IC<sub>50</sub> of 6.5 μg/ml and a leishmanicidal LC<sub>50</sub> of 9.06 μg/ml after 3 hours of exposure. Cytotoxic effects on macrophages were dose- and time-dependent. These findings suggest that recombinant Maurolipin possesses growth-inhibitory and apoptosis-inducing properties, highlighting its potential as a novel therapeutic agent for leishmaniasis.</p>

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The recombinant protein of scorpion venom phospholipase A2 exhibits potential anti-leishmanial activity

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月27日

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  • Parisa Soltan-Alinejad,
  • Amin Ramezani,
  • Qasem Asgari,
  • Hamzeh Alipour,
  • Aboozar Soltani,
  • Mohammad Saleh Bahreini,
  • Mahmood Nikbakhtzadeh,
  • Kourosh Azizi

摘要

The venom of scorpions contains a diverse array of bioactive compounds, including mucoproteins, nucleotides, and enzymes. Among these, phospholipase A2 (PLA2) plays a critical role in hydrolyzing plasma membrane phospholipids, leading to the release of fatty acids and lysophospholipids. In this study, characterized Maurolipin was selected as a candidate for recombinant protein production and evaluation of its anti-leishmanial activity. The recombinant protein was expressed in Escherichia coli strain Origami (DE3) and purified using a Ni-NTA resin column. The anti-parasitic activity of Maurolipin was tested against Leishmania major promastigotes, the causative agent of zoonotic cutaneous leishmaniasis (ZCL). The growth inhibitory effect was assessed across a range of concentrations (40 to 0.07 μg/ml). Leishmanicidal activity was determined by propidium iodide (PI) staining and flow cytometry, while cytotoxicity to RAW 264.7 macrophages was evaluated using an MTT assay. Maurolipin exhibited potent anti-leishmanial effects, with a 24-hour growth inhibition IC50 of 6.5 μg/ml and a leishmanicidal LC50 of 9.06 μg/ml after 3 hours of exposure. Cytotoxic effects on macrophages were dose- and time-dependent. These findings suggest that recombinant Maurolipin possesses growth-inhibitory and apoptosis-inducing properties, highlighting its potential as a novel therapeutic agent for leishmaniasis.