RSV glycoprotein and genomic RNA dynamics reveal filament assembly prior to the plasma membrane
Daryll Vanover,
Daisy V. Smith,
Emmeline L. Blanchard,
Eric Alonas,
Jonathan L. Kirschman,
Aaron W. Lifland,
Chiara Zurla and
Philip J. Santangelo ()
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Daryll Vanover: Georgia Institute of Technology and Emory University
Daisy V. Smith: Georgia Institute of Technology and Emory University
Emmeline L. Blanchard: Georgia Institute of Technology and Emory University
Eric Alonas: Georgia Institute of Technology and Emory University
Jonathan L. Kirschman: Georgia Institute of Technology and Emory University
Aaron W. Lifland: Georgia Institute of Technology
Chiara Zurla: Georgia Institute of Technology and Emory University
Philip J. Santangelo: Georgia Institute of Technology and Emory University
Nature Communications, 2017, vol. 8, issue 1, 1-15
Abstract:
Abstract The human respiratory syncytial virus G protein plays an important role in the entry and assembly of filamentous virions. Here, we report the use of fluorescently labeled soybean agglutinin to selectively label the respiratory syncytial virus G protein in living cells without disrupting respiratory syncytial virus infectivity or filament formation and allowing for interrogations of respiratory syncytial virus virion assembly. Using this approach, we discovered that plasma membrane-bound respiratory syncytial virus G rapidly recycles from the membrane via clathrin-mediated endocytosis. This event is then followed by the dynamic formation of filamentous and branched respiratory syncytial virus particles, and assembly with genomic ribonucleoproteins and caveolae-associated vesicles prior to re-insertion into the plasma membrane. We demonstrate that these processes are halted by the disruption of microtubules and inhibition of molecular motors. Collectively, our results show that for respiratory syncytial virus assembly, viral filaments are produced and loaded with genomic RNA prior to insertion into the plasma membrane.
Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00732-z
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DOI: 10.1038/s41467-017-00732-z
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