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

被引:26
|
作者
Li, Guohui [1 ]
Sun, Chen [1 ]
Zhang, Junhong [1 ]
He, Yuanqing [1 ]
Chen, Huiqing [1 ]
Kong, Jie [1 ]
Huang, Guoping [1 ]
Chen, Keping [1 ]
Yao, Qin [1 ]
机构
[1] Jiangsu Univ, Inst Life Sci, Zhenjiang 212013, Peoples R China
基金
中国国家自然科学基金;
关键词
Bombyx mori parvo-like virus; NS1; Helicase; SITE-SPECIFIC ENDONUCLEASE; MINK DISEASE PARVOVIRUS; MINUTE VIRUS; GEL-ELECTROPHORESIS; DNA-SEQUENCES; IDENTIFICATION; BINDING; ATPASE; MOTIF; NS-1;
D O I
10.1007/s11262-009-0402-x
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
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 6xHis-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 6xHis-NS1 protein in vitro. Taken together, our results indicated that BmDNV-Z NS1 was a multifunctional protein, which may be involved with virus replication.
引用
收藏
页码:396 / 402
页数:7
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