Gulati, Ashutosh and Murthy, Abhinandan and Abraham, Ambily and Mohan, Kalyani and Natraj, Usha and Savithri, HS and Murthy, MRN (2016) Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly. In: VIROLOGY, 489 . pp. 34-43.
PDF
Vir_489_34_2016.pdf - Published Version Restricted to Registered users only Download (4MB) | Request a copy |
Abstract
The capsid protein (CP) of Sesbania mosaic virus (SeMV, a T=3 plant virus) consists of a disordered N-terminal R-domain and an ordered S-domain. Removal of the R-domain results in the formation of T=1 particles. In the current study, the R-domain was replaced with unrelated polypeptides of similar lengths: the B-domain of Staphylococcus aureus SpA, and SeMV encoded polypeptides P8 and P10. The chimeric proteins contained T=3 or larger virus-like particles (VLPs) and could not be crystallized. The presence of metal ions during purification resulted in a large number of heterogeneous nucleoprotein complexes. N Delta 65-B (R domain replaced with B domain) could also be purified in a dimeric form. Its crystal structure revealed T=1 particles devoid of metal ions and the B-domain was disordered. However, the B-domain was functional in N Delta 65-B VLPs, suggesting possible biotechnological applications. These studies illustrate the importance of N-terminal residues, metal ions and robustness of the assembly process. (C) 2015 Elsevier Inc. All rights reserved.
Item Type: | Journal Article |
---|---|
Publication: | VIROLOGY |
Publisher: | ACADEMIC PRESS INC ELSEVIER SCIENCE |
Additional Information: | Copy right for this article belongs to the ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA |
Keywords: | SeMV; Chimeric VLPs; Coat protein; SeMV assembly; Virus nano-particles; R-domain; S. aureus B-domain; SeMV polypeptides P10 and P8 |
Department/Centre: | Division of Biological Sciences > Biochemistry Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 02 Apr 2016 07:26 |
Last Modified: | 02 Apr 2016 07:26 |
URI: | http://eprints.iisc.ac.in/id/eprint/53561 |
Actions (login required)
View Item |