Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly

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.

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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

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