Nipah Virus C Protein Recruits Tsg101 to Promote the Efficient Release of Virus in an ESCRT-Dependent Pathway

Arnold Park, Tatyana Yun, Frederic Vigant, Olivier Pernet, Sohui T. Won, Brian E. Dawes, Wojciech Bartkowski, Alexander N. Freiberg, Benhur Lee

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

The budding of Nipah virus, a deadly member of the Henipavirus genus within the Paramyxoviridae, has been thought to be independent of the host ESCRT pathway, which is critical for the budding of many enveloped viruses. This conclusion was based on the budding properties of the virus matrix protein in the absence of other virus components. Here, we find that the virus C protein, which was previously investigated for its role in antagonism of innate immunity, recruits the ESCRT pathway to promote efficient virus release. Inhibition of ESCRT or depletion of the ESCRT factor Tsg101 abrogates the C enhancement of matrix budding and impairs live Nipah virus release. Further, despite the low sequence homology of the C proteins of known henipaviruses, they all enhance the budding of their cognate matrix proteins, suggesting a conserved and previously unknown function for the henipavirus C proteins.

Original languageEnglish (US)
Article numbere1005659
JournalPLoS pathogens
Volume12
Issue number5
DOIs
StatePublished - May 2016

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Molecular Biology
  • Genetics
  • Virology

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    Park, A., Yun, T., Vigant, F., Pernet, O., Won, S. T., Dawes, B. E., Bartkowski, W., Freiberg, A. N., & Lee, B. (2016). Nipah Virus C Protein Recruits Tsg101 to Promote the Efficient Release of Virus in an ESCRT-Dependent Pathway. PLoS pathogens, 12(5), [e1005659]. https://doi.org/10.1371/journal.ppat.1005659