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J. Biol. Chem., Vol. 276, Issue 33, 30948-30955, August 17, 2001

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Effect of Osmolytes and Chaperone-like Action of P-protein on Folding of Nucleocapsid Protein of Chandipura Virus^*

Amitabha Majumder^§, Soumen Basak^§, Tamal Raha, Santanu Pal Chowdhury, Dhrubajyoti Chattopadhyay^¶, and Siddhartha Roy^**

From the  Department of Biochemistry and the Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology, University College of Science, University of Calcutta, 35 Ballygunge Circular Road, Calcutta 700 019, India and the  Department of Biophysics, Bose Institute, P 1/12 CIT. Scheme VII M, Calcutta 700 054, India

Amino acid sequences of nucleocapsid proteins are mostly conserved among different rhabdoviruses. The protein plays a common functional role in different RNA viruses by enwrapping the viral genomic RNA in an RNase-resistant form. Upon expression of the nucleocapsid protein alone in COS cells and in bacteria, it forms large insoluble aggregates. In this work, we have reported for the first time the full-length cloning of the N gene of Chandipura virus and its expression in Escherichia coli in a soluble monomeric form and purification using nonionic detergents. The biological activity of the soluble recombinant protein has been tested, and it was found to possess efficient RNA-binding ability. The state of aggregation of the recombinant protein was monitored using light scattering. In the absence of nonionic detergents, it formed large aggregates. Aggregation was significantly reduced in the presence of osmolytes such as D-sorbitol. Aggregate formation was suppressed in the presence of another viral product, phosphoprotein P, in a chaperone-like manner. Both the osmolyte and phosphoprotein P also suppressed aggregation to a great extent during refolding from a guanidine hydrochloride-denatured form. The function of the phosphoprotein and osmolyte appears to be synergistic to keep the N-protein in a soluble biologically competent form in virus-infected cells.

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