TY - JOUR
T1 - Nipah Virus C Protein Recruits Tsg101 to Promote the Efficient Release of Virus in an ESCRT-Dependent Pathway
AU - Park, Arnold
AU - Yun, Tatyana
AU - Vigant, Frederic
AU - Pernet, Olivier
AU - Won, Sohui T.
AU - Dawes, Brian E.
AU - Bartkowski, Wojciech
AU - Freiberg, Alexander N.
AU - Lee, Benhur
N1 - Publisher Copyright:
© 2016 Park et al.
PY - 2016/5
Y1 - 2016/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84973300827&partnerID=8YFLogxK
U2 - 10.1371/journal.ppat.1005659
DO - 10.1371/journal.ppat.1005659
M3 - Article
C2 - 27203423
AN - SCOPUS:84973300827
SN - 1553-7366
VL - 12
JO - PLoS Pathogens
JF - PLoS Pathogens
IS - 5
M1 - e1005659
ER -