Abstract
The Rift Valley fever virus is responsible for periodic, explosive epizootics throughout sub-Saharan Africa. The development of therapeutics targeting this virus is difficult due to a limited understanding of the viral replicative cycle. Utilizing a virus-like particle system, we have established roles for each of the viral structural components in assembly, release, and virus infectivity. The envelope glycoprotein, Gn, was discovered to be necessary and sufficient for packaging of the genome, nucleocapsid protein and the RNA-dependent RNA polymerase into virus particles. Additionally, packaging of the genome was found to be necessary for the efficient release of particles, revealing a novel mechanism for the efficient generation of infectious virus. Our results identify possible conserved targets for development of anti-phlebovirus therapies.
Highlights
Rift Valley fever virus (RVFV) is an aerosol- and mosquitoborne virus endemic to sub-Saharan Africa [1]
Rift Valley fever virus-like particle (RVF-VLP) were produced by expression of an S segment-based minigenome, N, RNA-dependent RNA polymerase (RdRp), Gn, and Gc in BSRT7/5 cells
RVFV and RVF-VLPs were harvested by ultracentrifugation and analyzed for particle morphology by transmission electron (Fig. 1) and protein composition by immunoblot (Fig. 2)
Summary
Rift Valley fever virus (RVFV) is an aerosol- and mosquitoborne virus endemic to sub-Saharan Africa [1]. RVFV causes periodic, explosive epizootics, affecting livestock and humans [1]. Most humans infected with RVFV have a flulike illness [1]. A small percentage of cases are more severe and include manifestations such as hemorrhagic disease and encephalitis [3,4,5]. Despite the severity of the disease to the economy and human health, there are no USDA or FDAapproved therapeutic or prophylactic treatments. A better understanding of the RVFV replication cycle may lead to the identification of novel therapeutic targets. We have identified roles for each of the viral structural components in the assembly and release of RVFV and have identified a potential conserved target for therapeutic development
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