Molecular characterization of nonstructural protein NS38 of grass carp reovirus.
Viral nonstructural proteins in both enveloped and non-enveloped viruses play important roles in viral replication. Protein NS38 of Grass carp reovirus (GCRV), has been deduced to be a non-structural protein, and, consistent with other reoviruses, is considered to cooperate with the NS80 protein in viral particle assembly. To investigate the molecular basis of the role of NS38, a complete protein was expressed in E.coli for the first time. It was found that there is a better expression of NS38 induced with IPTG at 28 °C rather than 37 °C. In addition, the antiserum of NS38 prepared with purified fusion protein and injected into rabbit could be used for detecting NS38 protein expression in GCRV infected cell lysate, while there is not any reaction crossed with purified virus particle, confirming NS38 is not a component of the viral structural protein. The result reported in this study will provide evidence for further viral protein-protein and protein-RNA interaction in dsRNA viruses replication.
State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Ling
L
Shao
Chao
C
Fan
Ewa
E
Maj
Qin
Q
Fang
D000818:Animals; D000914:Antibodies, Viral / Q000276:immunology*; D002347:Carps / Q000821:virology*; D002460:Cell Line; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D011817:Rabbits; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D012087:Reoviridae / Q000235:genetics*; D017361:Viral Nonstructural Proteins / Q000235:genetics*
D000914:Antibodies, Viral; D011994:Recombinant Proteins; D017361:Viral Nonstructural Proteins