Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V
AuthorAtkinson, SC; Audsley, MD; Lieu, KG; Marsh, GA; Thomas, DR; Heaton, SM; Paxman, JJ; Wagstaff, KM; Buckle, AM; Moseley, GW; ...
Source TitleScientific Reports
PublisherNATURE PUBLISHING GROUP
AffiliationBiochemistry and Molecular Biology
Microbiology and Immunology
Document TypeJournal Article
CitationsAtkinson, S. C., Audsley, M. D., Lieu, K. G., Marsh, G. A., Thomas, D. R., Heaton, S. M., Paxman, J. J., Wagstaff, K. M., Buckle, A. M., Moseley, G. W., Jans, D. A. & Borg, N. A. (2018). Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. SCIENTIFIC REPORTS, 8 (1), https://doi.org/10.1038/s41598-017-18742-8.
Access StatusOpen Access
Hendra virus (HeV) is a paramyxovirus that causes lethal disease in humans, for which no vaccine or antiviral agent is available. HeV V protein is central to pathogenesis through its ability to interact with cytoplasmic host proteins, playing key antiviral roles. Here we use immunoprecipitation, siRNA knockdown and confocal laser scanning microscopy to show that HeV V shuttles to and from the nucleus through specific host nuclear transporters. Spectroscopic and small angle X-ray scattering studies reveal HeV V undergoes a disorder-to-order transition upon binding to either importin α/β1 or exportin-1/Ran-GTP, dependent on the V N-terminus. Importantly, we show that specific inhibitors of nuclear transport prevent interaction with host transporters, and reduce HeV infection. These findings emphasize the critical role of host-virus interactions in HeV infection, and potential use of compounds targeting nuclear transport, such as the FDA-approved agent ivermectin, as anti-HeV agents.
- Click on "Export Reference in RIS Format" and choose "open with... Endnote".
- Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References