| 论文题目: | Characteristics of Nucleocytoplasmic Transport of H1N1 Influenza A Virus Nuclear Export Protein |
|---|---|
| 作者: | Gao Shengyan, Wang Shanshan, Cao Shuai, Sun Lei, Li Jing, Bi Yuhai, George F. Gao, Liu Wenjun* |
| 联系作者: | Liu Wenjun* |
| 刊物名称: | Journal of Virology |
| 期: | 88 |
| 卷: | 13 |
| 页: | 7455-7463 |
| 年份: | 2014 |
| 影响因子: | 4.855 |
| 论文下载: | 下载地址 |
| 摘要: | The influenza A virus nuclear export protein (NEP) plays crucial roles in the nuclear export of the viral ribonucleoprotein complex through the chromosome region maintenance 1 (CRM1)-mediated cellular protein transport system. However, the detailed mechanism of NEP nucleocytoplasmic trafficking remains incompletely understood. Here, we investigated the subcellular localization of NEP from two strains of H1N1 influenza A virus and found that 2009 swine-origin H1N1 influenza A virus A/California/ 04/2009 (CA04) NEP displayed a distinct cellular distribution pattern, forming unique nuclear aggregates, compared to A/WSN/33 (H1N1) (WSN) NEP. Characterization of the nucleocytoplasmic transport pathways of these two NEPs showed that they both enter the nucleus by passive diffusion but are exported through the nuclear export receptor CRM1-mediated pathway with different efficiencies. The two identified nuclear export signals (NESs) on the two NEPs functioned similarly despite differences in their amino acid sequences. Using a two-hybrid assay, we confirmed that the CA04 NEP interacts less efficiently with CRM1 and that a threonine residue at position 48 is responsible for the nuclear aggregation. The present study revealed the dissimilarity in subcellular NEP transport processes between the 2009 pandemic (H1N1) influenza A virus CA04 and the laboratory- adapted H1N1 virus WSN and uncovered the mechanism responsible for this difference. |
京公网安备 11010502044263号