Laboratory of protein engineering, Beijing Institute of Biotechnology, Beijing 100071, PR China.
Virol J. 2009 Dec 9;6:218. doi: 10.1186/1743-422X-6-218.
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 beta-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.
NS1 蛋白是流感 A 病毒唯一编码的非结构蛋白，通过调节许多病毒和宿主细胞过程，对疾病发病机制有重要贡献。从流感 A 中与 NS1 相互作用的蛋白质的双杂交筛选产生了生长停滞特异性蛋白 8。Gas8 与 NS1 在体外和体内相关。缺失分析表明，Gas8 的 N 端 260 个氨基酸能够与 NS1 相互作用，并且 NS1 的 RNA 结合域和效应子域都不足以进行 NS1 相互作用。我们还发现肌动蛋白、肌球蛋白和 drebrin 与 Gas8 相互作用。从转染细胞的提取物中可以共免疫沉淀 NS1 和β-肌动蛋白蛋白。此外，肌动蛋白和 Gas8 在质膜上共定位。这些结果与 Gas8 蛋白的可能功能及其在流感病毒释放中的相关性有关。
