Laboratory of Biophysics, Wageningen University, 6703 HA Wageningen, The Netherlands.
Eur Biophys J. 2010 Mar;39(4):541-50. doi: 10.1007/s00249-009-0523-0. Epub 2009 Aug 13.
During recent decades, bacteriophages have been at the cutting edge of new developments in molecular biology, biophysics, and, more recently, bionanotechnology. In particular filamentous viruses, for example bacteriophage M13, have a virion architecture that enables precision building of ordered and defect-free two and three-dimensional structures on a nanometre scale. This could not have been possible without detailed knowledge of coat protein structure and dynamics during the virus reproduction cycle. The results of the spectroscopic studies conducted in our group compellingly demonstrate a critical role of membrane embedment of the protein both during infectious entry of the virus into the host cell and during assembly of the new virion in the host membrane. The protein is effectively embedded in the membrane by a strong C-terminal interfacial anchor, which together with a simple tilt mechanism and a subtle structural adjustment of the extreme end of its N terminus provides favourable thermodynamical association of the protein in the lipid bilayer. This basic physicochemical rule cannot be violated and any new bionanotechnology that will emerge from bacteriophage M13 should take this into account.
近几十年来,噬菌体一直处于分子生物学、生物物理学,以及最近的生物纳米技术新发展的前沿。特别是丝状病毒,例如噬菌体 M13,其病毒粒子结构能够在纳米尺度上精确构建有序且无缺陷的二维和三维结构。如果没有在病毒繁殖周期中对衣壳蛋白结构和动力学的详细了解,这是不可能实现的。我们小组进行的光谱学研究结果有力地证明了蛋白质在病毒感染进入宿主细胞和在宿主膜中组装新病毒粒子期间的膜嵌入的关键作用。该蛋白质通过强 C 末端界面锚有效地嵌入在膜中,该界面锚与简单的倾斜机制以及其 N 末端的极端结构细微调整一起,为蛋白质在脂质双层中的有利热力学缔合提供了条件。这个基本的物理化学规则不能被违反,任何源自噬菌体 M13 的新生物纳米技术都应该考虑到这一点。