Tracking the Fate of Genetically Distinct Vesicular Stomatitis Virus Matrix Proteins Highlights the Role for Late Domains in Assembly

Journal of Virology
Timothy K Soh, Sean P J Whelan

Abstract

Vesicular stomatitis virus (VSV) assembly requires condensation of the viral ribonucleoprotein (RNP) core with the matrix protein (M) during budding from the plasma membrane. The RNP core comprises the negative-sense genomic RNA completely coated by the nucleocapsid protein (N) and associated by a phosphoprotein (P) with the large polymerase protein (L). To study the assembly of single viral particles, we tagged M and P with fluorescent proteins. We selected from a library of viruses with insertions in the M gene a replication-competent virus containing a fluorescent M and combined that with our previously described virus containing fluorescent P. Virus particles containing those fusions maintained the same bullet shape appearance as wild-type VSV but had a modest increase in particle length, reflecting the increased genome size. Imaging of the released particles revealed a variation in the amount of M and P assembled into the virions, consistent with a flexible packaging mechanism. We used the recombinants to further study the importance of the late domains in M, which serve to recruit the endosomal sorting complex required for transport (ESCRT) machinery during budding. Mutations in late domains resulted in the accumulation o...Continue Reading

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Citations

May 24, 2019·Journal of Virology·Xin ZhouZhenghe Li
Mar 10, 2016·Viruses·Ronan N RouxelMichel Brémont
Aug 9, 2020·Proceedings of the National Academy of Sciences of the United States of America·Yuan-Lin KangTom Kirchhausen
Jul 1, 2016·Annual Review of Phytopathology·Andrew O Jackson, Zhenghe Li
Sep 3, 2020·Viruses·Christiane RiedelKarl-Klaus Conzelmann
Nov 10, 2017·Cell Host & Microbe·Matthijs RaabenSean P Whelan

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