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| Content Provider | Springer Nature : BioMed Central |
|---|---|
| Author | Yanai, Mako Sakai, Madoka Makino, Akiko Tomonaga, Keizo |
| Abstract | Background Borna disease virus (BoDV), which has a negative-sense, single-stranded RNA genome, causes persistent infection in the cell nucleus. The nuclear export signal (NES) of the viral nucleoprotein (N) consisting of leucine at positions 128 and 131 and isoleucine at positions 133 and 136 overlaps with one of two predicted binding sites for the viral phosphoprotein (P). A previous study demonstrated that higher expression of BoDV-P inhibits nuclear export of N; however, the function of N NES in the interaction with P remains unclear. We examined the subcellular localization, viral polymerase activity, and P-binding ability of BoDV-N NES mutants. We also characterized a recombinant BoDV (rBoDV) harboring an NES mutation of N. Results BoDV-N with four alanine-substitutions in the leucine and isoleucine residues of the NES impaired its cytoplasmic localization and abolished polymerase activity and P-binding ability. Although an alanine-substitution at position 131 markedly enhanced viral polymerase activity as determined by a minigenome assay, rBoDV harboring this mutation showed expression of viral RNAs and proteins relative to that of wild-type rBoDV. Conclusions Our results demonstrate that BoDV-N NES has a dual function in BoDV replication, i.e., nuclear export of N and an interaction with P, affecting viral polymerase activity in the nucleus. |
| Related Links | https://virologyj.biomedcentral.com/counter/pdf/10.1186/s12985-017-0793-6.pdf |
| Ending Page | 7 |
| Page Count | 7 |
| Starting Page | 1 |
| File Format | HTM / HTML |
| DOI | 10.1186/s12985-017-0793-6 |
| Journal | Virology Journal |
| Issue Number | 1 |
| Volume Number | 14 |
| Language | English |
| Publisher | BioMed Central |
| Publisher Date | 2017-07-11 |
| Access Restriction | Open |
| Subject Keyword | Virology Borna disease virus Nucleocytoplasmic shuttling Nuclear export signal Nucleoprotein-phosphoprotein interaction Polymerase activity |
| Content Type | Text |
| Resource Type | Article |
| Subject | Virology Infectious Diseases |
| Journal Impact Factor | 4/2023 |
| 5-Year Journal Impact Factor | 3.8/2023 |
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