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

• Published in: PLoS pathogens 2016-05, Vol.12 (5), p.e1005659-e1005659
• Main Authors: Park, Arnold, Yun, Tatyana, Vigant, Frederic, Pernet, Olivier, Won, Sohui T, Dawes, Brian E, Bartkowski, Wojciech, Freiberg, Alexander N, Lee, Benhur
• Format: Article
• Language: English
• Subjects: Analysis; Biology and life sciences; Blotting, Western; Budding (Reproduction); DNA-Binding Proteins - metabolism; Endosomal Sorting Complexes Required for Transport - metabolism; Epidemics; Funding; HEK293 Cells; Henipavirus Infections - metabolism; Humans; Immunoprecipitation; Medicine and Health Sciences; Microscopy; Microscopy, Confocal; Microscopy, Electron, Transmission; Molecular weight; Mortality; Nipah virus; Nipah Virus - physiology; Paramyxoviridae; Phosphoproteins - metabolism; Proteins; Research and analysis methods; Risk factors; Transcription Factors - metabolism; Viral Proteins - metabolism; Virus Release - physiology; Viruses
• ISSN: 1553-7374; 1553-7366; 1553-7374
• DOI: 10.1371/journal.ppat.1005659

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.