Bluetongue Virus Nonstructural Protein 3 Orchestrates Virus Maturation and Drives Non-Lytic Egress via Two Polybasic Motifs
| Autor: | Sophie Jegouic, Thomas Labadie, Polly Roy |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
viruses Amino Acid Motifs 030106 microbiology Mutant Viral Nonstructural Proteins Virus Replication Bluetongue Article Virus 03 medical and health sciences symbols.namesake Cricetinae Virology Virus maturation Animals Amino Acid Sequence Virus Release polybasic motif NS3 Sheep Chemistry virus budding Virus Assembly Endoplasmic reticulum Virion RNA biochemical phenomena metabolism and nutrition Golgi apparatus Cell biology Protein Transport 030104 developmental biology Infectious Diseases Lytic cycle Mutagenesis Site-Directed symbols non-structural protein Sequence Alignment Bluetongue virus |
| Zdroj: | Viruses Volume 11 Issue 12 |
| ISSN: | 1999-4915 |
| Popis: | Bluetongue virus (BTV) is an arthropod-borne virus that infects domestic and wild ruminants. The virion is a non-enveloped double-layered particle with an outer capsid that encloses a core containing the segmented double-stranded RNA genome. Although BTV is canonically released by cell lysis, it also exits non-lytically. In infected cells, the BTV nonstructural glycoprotein 3 (NS3) is found to be associated with host membranes and traffics from the endoplasmic reticulum through the Golgi apparatus to the plasma membrane. This suggests a role for NS3 in BTV particle maturation and non-lytic egress. However, the mechanism by which NS3 coordinates these events has not yet been elucidated. Here, we identified two polybasic motifs (PMB1/PMB2), consistent with the membrane binding. Using site-directed mutagenesis, confocal and electron microscopy, and flow cytometry, we demonstrated that PBM1 and PBM2 mutant viruses retained NS3 either in the Golgi apparatus or in the endoplasmic reticulum, suggesting a distinct role for each motif. Mutation of PBM2 motif decreased NS3 export to the cell surface and virus production. However, both mutant viruses produced predominantly inner core particles that remained close to their site of assembly. Together, our data demonstrates that correct trafficking of the NS3 protein is required for virus maturation and release. |
| Databáze: | OpenAIRE |
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