Classic swine fever is a highly contagious and often fatal viral disease that is caused by the classical swine fever virus (CSFV). Protein p7 of CFSV is a prototype of viroporin, a family of small, highly hydrophobic proteins postulated to modulate virus-host interactions during the processes of virus entry, replication and assembly. It has been shown that CSFV p7 displays substantial ion channel activity when incorporated into membrane systems, but a deep rationalization of the size and dynamics of the induced pores is yet to emerge. Here, we use high-resolution conductance measurements and current fluctuation analysis to demonstrate that CSFV p7 channels are ruled by equilibrium conformational dynamics involving protein-lipid interactions. Atomic force microscopy (AFM) confirms the existence of a variety of pore sizes and their tight regulation by solution pH. We conclude that p7 viroporin forms subnanometric channels involved in virus propagation, but also much larger pores (1–10 nm in diameter) with potentially significant roles in virus pathogenicity. Our findings provide new insights into the sources of noise in protein electrochemistry and demonstrate the existence of slow complex dynamics characteristic of crowded systems like biomembrane surfaces.

经典猪瘟是一种由经典猪瘟病毒（CSFV）引起的高度传染性且通常是致命的病毒性疾病。CFSV蛋白p7是viroporin的原型，viroporin是一类小而高度疏水的蛋白，被假定在病毒进入，复制和组装过程中调节病毒与宿主的相互作用。已经显示出，当将CSFV p7掺入膜系统中时，它显示出实质性的离子通道活性，但是尚未出现对诱导孔的尺寸和动力学的深入合理化。在这里，我们使用高分辨率电导测量和电流波动分析来证明CSFV p7通道受涉及蛋白质-脂质相互作用的平衡构象动力学的支配。原子力显微镜（AFM）证实了各种孔径的存在及其通过溶液pH的严格调节。我们得出的结论是，p7维罗帕林形成了参与病毒传播的亚纳米通道，但也形成了较大的孔（直径1-10 nm），在病毒致病性中具有潜在的重要作用。我们的发现为蛋白质电化学中的噪声来源提供了新的见解，并证明了拥挤系统（如生物膜表面）的慢速复杂动力学特征的存在。