Elucidating the functional aspects of different domains of bean common mosaic virus coat protein.

Elucidating the functional aspects of different domains of bean common mosaic virus coat protein.
Virus Res. 2019 Sep 13;:197755
Authors: Kumar S, Karmakar R, Garg DK, Gupta I, Patel AK
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 amino acids position in it. The 3'UTR RNA of the virus showed high binding affinity with the RNA binding domain in comparison 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.
PMID: 31525400 [PubMed - as supplied by publisher]

Source: Virus Research - September 12, 2019 Category: Virology Authors: Kumar S, Karmakar R, Garg DK, Gupta I, Patel AK Tags: Virus Res Source Type: research