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Covalent linkage of bacterial voltage-gated sodium channels

机译：细菌电压门控钠通道的共价键

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Bacterial sodium channels are important models for understanding ion permeation and selectivity. However, their homotetrameric structure limits their use as models for understanding the more complex eukaryotic voltage-gated sodium channels (which have a pseudo-heterotetrameric structure formed from an oligomer composed of four domains). To bridge this gap we attempted to synthesise oligomers made from four covalently linked bacterial sodium channel monomers and thus resembling their eukaryotic counterparts. Western blot analyses revealed NaChBac oligomers to be inherently unstable whereas intact expression of NavMs oligomers was possible. Immunodectection using confocal microscopy and electrophysiological characterisation of NavMs tetramers confirmed plasma membrane localisation and equivalent functionality with wild type NavMs channels when expressed in human embryonic kidney cells. This study has generated new tools for the investigation of eukaryotic channels. The successful covalent linkage of four bacterial Nav channel monomers should permit the introduction of radial asymmetry into the structure of bacterial Nav channels and enable the known structures of these channels to be used to gain unique insights into structure-function relationships of their eukaryotic counterparts.
机译：细菌钠通道是了解离子渗透性和选择性的重要模型。但是，它们的同四聚体结构限制了它们用作理解更复杂的真核电压门控钠通道（其具有由四个结构域组成的低聚物形成的假异四聚体结构）的模型的用途。为了弥合这一差距，我们尝试合成由四个共价连接的细菌钠通道单体制成的寡聚物，因此类似于它们的真核对应物。蛋白质印迹分析显示NaChBac寡聚物固有地不稳定，而NavMs寡聚物的完整表达是可能的。使用共聚焦显微镜进行的免疫检测和NavMs四聚体的电生理特性证实，当在人胚胎肾细胞中表达时，质膜定位和野生型NavMs通道具有同等功能。这项研究已经产生了用于调查真核通道的新工具。四个细菌Nav通道单体的成功共价连接应允许在细菌Nav通道的结构中引入径向不对称性，并使这些通道的已知结构可用于获得对其真核对应物的结构-功能关系的独特见解。

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