Extensive characterization of a lentiviral-derived stable cell line expressing rabbit hemorrhagic disease virus VPg protein

2016 ◽  
Vol 237 ◽  
pp. 86-91 ◽  
Author(s):  
Jie Zhu ◽  
Qiuhong Miao ◽  
Yonggui Tan ◽  
Huimin Guo ◽  
Chuanfeng Li ◽  
...  
Keyword(s):  
Cell Line ◽  
Disease Virus ◽  
Stable Cell Line ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease

scholarly journals ATP Binding and ATPase Activities Associated with Recombinant Rabbit Hemorrhagic Disease Virus 2C-Like Polypeptide

2000 ◽  
Vol 74 (22) ◽  
pp. 10846-10851 ◽  
Author(s):  
M. Soledad Marín ◽  
Rosa Casais ◽  
José M. Martín Alonso ◽  
Francisco Parra
Keyword(s):  
Disease Virus ◽  
Site Directed Mutagenesis ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Atp Binding ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

ABSTRACT The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 polyprotein cleavage product has been expressed inEscherichia coli as a glutathione S-transferase (GST) fusion protein. The recombinant GST-Δ2C protein showed in vitro ATP-binding and ATPase activities. Site-directed mutagenesis studies of the conserved residues G522 and T529 in motif A, D566 and E567 in motif B, and K600 in motif C were also performed. These results provide the first experimental characterization of a 2C-like ATPase activity in a member of the Caliciviridae.

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