| Autor: |
Yu Mengbin, Zhu Xudong, Zhang Chuanfu, Yang Zhixin, Zhu Qingyu, Zhou Xiaowei, Xu Long, Zhao Lixia, Zhang Yingying, Zhao Xinghui, Huang Peitang |
| Jazyk: |
angličtina |
| Rok vydání: |
2009 |
| Předmět: |
|
| Zdroj: |
Virology Journal, Vol 6, Iss 1, p 218 (2009) |
| Druh dokumentu: |
article |
| ISSN: |
1743-422X |
| DOI: |
10.1186/1743-422X-6-218 |
| Popis: |
Abstract NS1 protein is the only non-structural protein encoded by the influenza A virus, and it contributes significantly to disease pathogenesis by modulating many virus and host cell processes. A two-hybrid screen for proteins that interact with NS1 from influenza A yielded growth arrest-specific protein 8. Gas8 associated with NS1 in vitro and in vivo. Deletion analysis revealed that the N-terminal 260 amino acids of Gas8 were able to interact with NS1, and neither the RNA-binding domain nor the effector domain of NS1 was sufficient for the NS1 interaction. We also found that actin, myosin, and drebrin interact with Gas8. NS1 and β-actin proteins could be co-immunoprecipitated from extracts of transfected cells. Furthermore, actin and Gas8 co-localized at the plasma membrane. These results are discussed in relation to the possible functions of Gas8 protein and their relevance in influenza virus release. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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