Li Guohui, Sun Chen, Zhang Junhong, He Yuanqing, Chen Huiqing, Kong Jie, Huang Guoping, Chen Keping, Yao Qin
Institute of Life Sciences, Jiangsu University, Zhenjiang, China.
Virus Genes. 2009 Dec;39(3):396-402. doi: 10.1007/s11262-009-0402-x. Epub 2009 Oct 9.
NS1 gene of Bombyx mori parvo-like virus (China Zhenjiang isolate, BmDNV-Z) codes a predicted 316-amino acid protein, but its function remains unknown. Results of the current study showed that purified recombinant 6 x His-NS1 protein possesses ATP binding, ATPase, DNA binding, and helicase activities. Only one protein was captured in infected Bombyx mori midgut cells against NS1 target protein by employing co-immunoprecipitation, which was identified to be a viral protein by mass spectrometry. The NS1-interacting protein is encoded by BmDNV-Z ORF4 and its molecular is about 100 kD. Analysis of His pull-down confirmed that binding of identified viral protein to purified recombinant 6 x His-NS1 protein in vitro. Taken together, our results indicated that BmDNV-Z NS1 was a multifunctional protein, which may be involved with virus replication.
家蚕细小病毒样病毒(中国镇江分离株,BmDNV-Z)的NS1基因编码一种预测的316个氨基酸的蛋白质,但其功能尚不清楚。本研究结果表明,纯化的重组6×His-NS1蛋白具有ATP结合、ATP酶、DNA结合和解旋酶活性。通过免疫共沉淀,在感染家蚕中肠细胞中仅捕获到一种针对NS1靶蛋白的蛋白,经质谱鉴定为病毒蛋白。NS1相互作用蛋白由BmDNV-Z ORF4编码,其分子量约为100 kD。His下拉分析证实了体外鉴定的病毒蛋白与纯化的重组6×His-NS1蛋白的结合。综上所述,我们的结果表明BmDNV-Z NS1是一种多功能蛋白,可能参与病毒复制。