Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK.
J Mol Biol. 2011 May 6;408(3):408-19. doi: 10.1016/j.jmb.2011.02.040. Epub 2011 Mar 2.
We describe the cryo-electron microscopy structure of bacteriophage MS2 bound to its receptor, the bacterial F-pilus. The virus contacts the pilus at a capsid 5-fold vertex, thus locating the surface-accessible portion of the single copy of the pilin-binding maturation protein present in virions. This arrangement allows a 5-fold averaged map to be calculated, showing for the first time in any virus-receptor complex the nonuniform distribution of RNA within the capsid. Strikingly, at the vertex that contacts the pilus, a rod of density that may include contributions from both genome and maturation protein sits above a channel that goes through the capsid to the outside. This density is reminiscent of the DNA density observed in the exit channel of double-stranded DNA phages, suggesting that the RNA-maturation protein complex is poised to leave the capsid as the first step of the infection process.
我们描述了噬菌体 MS2 与其受体——细菌 F 菌毛结合的冷冻电子显微镜结构。病毒在衣壳五重对称顶点处与菌毛接触,从而定位存在于病毒颗粒中的单拷贝菌毛结合成熟蛋白的表面可及部分。这种排列允许计算出五重平均图,首次在任何病毒-受体复合物中显示衣壳内 RNA 的非均匀分布。引人注目的是,在与菌毛接触的顶点处,一个可能包含基因组和成熟蛋白贡献的密度棒位于穿过衣壳通向外部的通道上方。这种密度类似于在双链 DNA 噬菌体的出口通道中观察到的 DNA 密度,表明 RNA-成熟蛋白复合物准备离开衣壳,作为感染过程的第一步。