Nonkhwao Siriporn, Rungsa Prapenpuksiri, Buraphaka Hathairat, Klaynongsruang Sompong, Daduang Jureerut, Kornthong Napamanee, Daduang Sakda
Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand.
Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen 40002, Thailand.
Int J Mol Sci. 2023 Oct 1;24(19):14814. doi: 10.3390/ijms241914814.
is recognized for containing the allergenic proteins Sol g 1, 2, 3, and 4 in its venom. Remarkably, Sol g 2.1 exhibits hydrophobic binding and has a high sequence identity (83.05%) with Sol i 2 from . Notably, Sol g 2.1 acts as a mediator, causing paralysis in crickets. Given its structural resemblance and biological function, Sol g 2.1 may play a key role in transporting hydrophobic potent compounds, which induce paralysis by releasing the compounds through the insect's nervous system. To investigate this further, we constructed and characterized the recombinant Sol g 2.1 protein (rSol g 2.1), identified with LC-MS/MS. Circular dichroism spectroscopy was performed to reveal the structural features of the rSol g 2.1 protein. Furthermore, after treating crickets with venom, immunofluorescence and immunoblotting results revealed that the Sol g 2.1 protein primarily localizes to the neuronal cell membrane of the brain and thoracic ganglia, with distribution areas related to octopaminergic neuron cell patterns. Based on protein-protein interaction predictions, we found that the Sol g 2.1 protein can interact with octopamine receptors (OctRs) in neuronal cell membranes, potentially mediating Sol g 2.1's localization within cricket central nervous systems. Here, we suggest that Sol g 2.1 may enhance paralysis in crickets by acting as carriers of active molecules and releasing them onto target cells through pH gradients. Future research should explore the binding properties of Sol g 2.1 with ligands, considering its potential as a transporter for active molecules targeting pest nervous systems, offering innovative pest control prospects.
因其毒液中含有变应原蛋白Sol g 1、2、3和4而被识别。值得注意的是，Sol g 2.1表现出疏水结合特性，并且与来自[未提及的来源]的Sol i 2具有较高的序列同一性（83.05%）。值得注意的是，Sol g 2.1作为一种介质，可导致蟋蟀麻痹。鉴于其结构相似性和生物学功能，Sol g 2.1可能在运输疏水性强效化合物中起关键作用，这些化合物通过昆虫的神经系统释放化合物来诱导麻痹。为了进一步研究这一点，我们构建并表征了通过LC-MS/MS鉴定的重组Sol g 2.1蛋白（rSol g 2.1）。进行圆二色光谱分析以揭示rSol g 2.1蛋白的结构特征。此外，在用[未提及的毒液]处理蟋蟀后，免疫荧光和免疫印迹结果显示，Sol g 2.1蛋白主要定位于大脑和胸神经节的神经元细胞膜，其分布区域与章鱼胺能神经元细胞模式相关。基于蛋白质-蛋白质相互作用预测，我们发现Sol g 2.1蛋白可与神经元细胞膜中的章鱼胺受体（OctRs）相互作用，这可能介导Sol g 2.1在蟋蟀中枢神经系统中的定位。在此，我们认为Sol g 2.1可能通过作为活性分子的载体并通过pH梯度将它们释放到靶细胞上而增强对蟋蟀的麻痹作用。未来的研究应探索Sol g 2.1与配体的结合特性，考虑到其作为靶向害虫神经系统的活性分子转运体的潜力，这为害虫防治提供了创新前景。
