Title
Elucidating the functional aspects of different domains of bean common mosaic virus coat protein
Author
Sunil Kumar, Ruma Karmakar, Dushyant Kumar Garg, Ishu Gupta, Ashok Kumar Patel
Year
2019
Journal
Virus Research
Abstract
The coat protein (CP) is the only structural protein present in the polyprotein of bean common mosaic virus. The well known characteristics of the CP are self-oligomerization and nucleic acid binding activity. The studies of the coat protein mutants revealed that the oligomeric property of CP solely depends on the amino-terminal residues and the nucleic acid binding domain present at the 194–202 residue position. The 3′UTR RNA of the virus showed high binding affinity with the RNA binding domain as compared to the 5′UTR RNA. Further, the intrinsic fluorescence study of the CP also suggested that the N- and C-terminal of CP contains a highly disordered region. The present study also illustrates that the coat protein contains a conserved RNA binding pocket among the potyviruses, but displays divergent oligomerization propensities due to the difference in residue at the N- and C-terminal.
Instrument
J-815
Keywords
Circular dichroism, Secondary structure, Chemical stability, Protein denaturation, Biochemistry