Žerovnik Eva
Department of Biochemistry and Molecular and Structural Biology, J. Stefan Institute, Ljubljana, Slovenia.
Front Chem. 2021 Feb 18;9:626059. doi: 10.3389/fchem.2021.626059. eCollection 2021.
Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell's signaling routes and fate. Such pore-forming proteins exist from bacteria to viruses and also shape host defense systems, including innate immunity. There is strong evidence that amyloid toxicity is also caused by prefibrillar oligomers making "amyloid pores" into cellular membranes. For most of the PFPs, a 2-step mechanism of protein-membrane interaction takes place on the "lipid rafts," membrane microdomains rich in gangliosides and cholesterol. In this mini-review paper, common traits of different PFPs are looked at. Possible ways for therapy of channelopathies and/or modulating immunity relevant to the new threat of SARS-CoV-2 infections could be learnt from such comparisons.
成孔蛋白（PFPs）几乎存在于生命的所有领域，通过破坏细胞膜，根据孔径大小，它们会导致离子失衡、小分子物质甚至蛋白质的外流/内流，影响细胞的信号通路和命运。这类成孔蛋白从细菌到病毒都有，并且也塑造宿主防御系统，包括先天免疫。有强有力的证据表明，淀粉样毒性也是由原纤维前体寡聚体在细胞膜上形成“淀粉样孔”所导致的。对于大多数成孔蛋白而言，蛋白质与膜的相互作用通过两步机制在“脂筏”上发生，脂筏是富含神经节苷脂和胆固醇的膜微区。在这篇小型综述论文中，我们探讨了不同成孔蛋白的共同特征。通过这样的比较，有望找到治疗通道病和/或调节与新型冠状病毒感染这一新威胁相关的免疫的可能方法。
