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家蚕细小病毒样病毒非结构蛋白NS1的特性分析

Characterization of Bombyx mori parvo-like virus non-structural protein NS1.

作者信息

Li Guohui, Sun Chen, Zhang Junhong, He Yuanqing, Chen Huiqing, Kong Jie, Huang Guoping, Chen Keping, Yao Qin

机构信息

Institute of Life Sciences, Jiangsu University, Zhenjiang, China.

出版信息

Virus Genes. 2009 Dec;39(3):396-402. doi: 10.1007/s11262-009-0402-x. Epub 2009 Oct 9.

Abstract

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.

摘要

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。

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