Asymmetric packaging of polymerases within vesicular stomatitis virus |
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| Authors: | Jeffery Hodges Xiaolin Tang Michael B. Landesman John B. Ruedas Anil Ghimire Manasa V. Gudheti Jacques Perrault Erik M. Jorgensen Jordan M. Gerton Saveez Saffarian |
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| Affiliation: | 1. Dept. of Physics and Astronomy, University of Utah, United States;2. Center for Cell and Genome Science, University of Utah, United States;3. Dept. of Biology, San Diego State University, United States;4. Vutara, Inc., Salt Lake City, UT, United States;5. Howard Hughes Medical Institute, United States;6. Dept. of Bioengineering, University of Utah, United States;g Dept. of Biology, University of Utah, United States |
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| Abstract: | 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. L and 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. |
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| Keywords: | VSV RdRP Polymerase PALM STORM AFM L protein P protein Viral replication |
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