| 论文题目: | Characterization of The Nucleocytoplasmic Shuttle of The Matrix Protein of Influenza B Virus |
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| 作者: | Cao Shuai#, Jiang Jingwen#, Li Jing, Li Yan, Yang Limin, Wang Shanshan, Yan Jinghua, George F Gao, Liu Wenjun* |
| 联系作者: | Liu Wenjun* |
| 刊物名称: | J Virol |
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| 年份: | 2014 |
| 影响因子: | 4.893 |
| 论文下载: | 下载地址 |
| 摘要: | Influenza B virus is an enveloped negative-strand RNA virus, that contributes considerably to annual influenza illnesses in human. The matrix protein of influenza B virus (BM1) acts as a cytoplasmic-nuclear shuttling protein during the early and late stages of infection. The mechanism of this intracellular transport of BM1 was revealed through the identification of two leucine-rich CRM1-dependent nuclear export signals (NESs) (3-14aa and 124-133aa), one bipartite nuclear localization signal (NLS) (76-94aa), and two phosphorylation sites (80T and 84S) in BM1. The biological function of the NLS and NES regions were determined through the observation of the intracellular distribution of EGFP-tagged signal peptides, and WT, NES-mutant and NLS-mutant EGFP-BM1. Furthermore, the NLS phosphorylation sites 80T and 84S, were found to be required for the nuclear accumulation of EGFP-NLS and for the efficient binding of EGFP-BM1 to human importin-alpha 1. Moreover, all of these regions/sites were required for the generation of viable influenza B virus in a 12-plasmid virus rescue system. IMPORTANCE: This study expands our understanding of the life cycle of influenza B virus by defining defines/presents the dynamic mechanism of the nucleocytoplasmic shuttle of BM1, and could provide a scientific basis for the development of anti-viral medication. |
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