Expression and Purification of Vaccinia Virus DNA Topoisomerase IB Produced in the Silkworm–Baculovirus Expression System

2019 ◽  
Vol 61 (8) ◽  
pp. 622-630 ◽  
Author(s):  
Jian Xu ◽  
Jae Man Lee ◽  
Tuneyuki Tatsuke ◽  
Takeru Ebihara ◽  
Akitsu Masuda ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Expression And Purification ◽  
Dna Topoisomerase ◽  
Baculovirus Expression ◽  
Topoisomerase Ib

scholarly journals Expression, Purification and Sublocalization of SARS-CoV Nucleocapsid Protein in Insect Cells

2004 ◽  
Vol 36 (11) ◽  
pp. 754-758 ◽  
Author(s):  
Ai-Xia Ren ◽  
You-Hua Xie ◽  
Yu-Ying Kong ◽  
Guan-Zhen Yang ◽  
Yao-Zhou Zhang ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Trichoplusia Ni ◽  
Insect Cells ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Functional Study ◽  
Expression And Purification ◽  
N Protein ◽  
Baculovirus Expression

Abstract The causative agent of severe acute respiratory syndrome (SARS) is a previously unidentified coronavirus, SARS-CoV. The nucleocapsid (N) protein of SARS-CoV is a major viral protein recognized by acute and early convalescent sera from SARS patients. To facilitate the studies on the function and structure of the N protein, this report describe the expression and purification of recombinant SARS-CoV N protein using the baculovirus expression system. Recombinant hexa-histidine-tagged N protein with a molecular mass of 47 kD was produced in insect cells. Recombinant N protein was purified to near homogeneity by Ni2+-NTA affinity chromatography. In addition, we examined the subcellular localization of the N protein by confocal microscopy in Trichoplusia ni BT1 Tn 5B1–4 cells infected with recombinant baculovirus. The N protein was found localized in the cytoplasm as well as in the nucleolus. The purified recombinant N protein can be used in further functional study of SARS-CoV.

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