Asymmetric packaging of polymerases within vesicular stomatitis virus

作者：Hodges Jeffery; Tang Xiaolin; Landesman Michael B; Ruedas John B; Ghimire Anil; Gudheti Manasa V; Perrault Jacques; Jorgensen Erik M; Gerton Jordan M; Saffarian Saveez^*

来源：Biochemical and Biophysical Research Communications, 2013, 440(2): 271-276.

DOI：10.1016/j.bbrc.2013.09.064

• VSV
• RdRP
• Polymerase
• PALM
• STORM
• AFM
• L protein
• P protein
• Viral replication

Vesicular stomatitis virus (VSV) is a prototypic negative sense single-stranded RNA virus. The bullet-shape appearance of the virion results from tightly wound helical turns of the nucleoprotein encapsidated RNA template (N-RNA) around a central cavity. Transcription and replication require polymerase complexes, which include a catalytic subunit L and a template-binding subunit P. Land P are inferred to be in the cavity, however lacking direct observation, their exact position has remained unclear. Using super-resolution fluorescence imaging and atomic force microscopy (AFM) on single VSV virions, we show that L and P are packaged asymmetrically towards the blunt end of the virus. The number of L and P proteins varies between individual virions and they occupy 57 +/- 12 nm of the 150 nm central cavity of the virus. Our finding positions the polymerases at the opposite end of the genome with respect to the only transcriptional promoter.

• 出版日期2013-10-18