P-Protein of Chandipura Virus Is an N-Protein-Specific Chaperone That Acts at the Nucleation Stage

Majumdar, A and Bhattacharya, R and Basak, S and Shaila, MS and Chattopadhyay, D and Roy, S (2004) P-Protein of Chandipura Virus Is an N-Protein-Specific Chaperone That Acts at the Nucleation Stage. In: Biochemistry, 43 (10). pp. 2863-2870.

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Abstract

The nucleocapsid protein N of Chandipura virus is prone to aggregation in vitro. We have shown that this aggregation occurs in two phases in a nucleation-dependent manner. Electron microscopy suggests that the aggregated state may have a ring-like structure. Using a GFP fusion, we have shown that the N-protein also aggregates in vivo. The P-protein suppresses the N-protein aggregation efficiently, both in vitro and in vivo. Increased lag phase in the presence of the P-protein suggests that chaperone-like action of the P-protein occurs before the nucleation event. The P-protein, however, does not exert any chaperone-like action against other proteins, suggesting that it binds to the N-protein specifically. Surface plasmon resonance and fluorescence enhancement indeed suggest that the P-protein binds tightly to the native N-protein. The P-protein is thus an N-protein-specific chaperone which inhibits the nucleation phase of N-protein aggregation, thus keeping a pool of encapsidation-competent N-protein for viral maturation.

Item Type:	Journal Article
Publication:	Biochemistry
Publisher:	American Chemical Society.
Additional Information:	Copyright of this article belongs to American Chemical Society.
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	19 Dec 2008 11:14
Last Modified:	19 Sep 2010 04:56
URI:	http://eprints.iisc.ac.in/id/eprint/17231

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