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.
journal_name
Virus Resjournal_title
Virus researchauthors
Kumar S,Karmakar R,Garg DK,Gupta I,Patel AKdoi
10.1016/j.virusres.2019.197755subject
Has Abstractpub_date
2019-11-01 00:00:00pages
197755eissn
0168-1702issn
1872-7492pii
S0168-1702(19)30386-7journal_volume
273pub_type
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