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Functional Characterization of Phosphorylation of the Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) Nucleocapsid Protein  

Lee, Chang-Hee (School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University)
Publication Information
Microbiology and Biotechnology Letters / v.37, no.3, 2009 , pp. 287-292 More about this Journal
Abstract
The nucleocapsid (N) protein of porcine reproductive and respiratory syndrome virus (PRRSV) is a basic multifunctional protein which has been reported to be a serine phosphoprotein with yet-identified functions. As a first step towards understanding the general role of N protein phosphorylation during virus replication, the non-phosphorylated mutant N gene was constructed by mutating all serine residues to alanine. This recombinant N protein was identified to be unphosphorylated, confirming that serine residues truly function as core amino acids responsible for N protein phosphorylation. The PRRSV N protein has been shown to possess the biological features of nuclear localization and N-N homodimerization which individually play critical roles in virus infection. In the present study, therefore, it was attempted to investigate whether these two properties of the N protein are modulated by its phosphorylation status. However, experimental results showed that the non-phosphorylated N protein was still present in the nucleus and nucleolus, and was able to associate with itself by non-covalent interactions. Taken together, the data suggest phosphorylation-independent regulation of N protein nuclear transport or oligomerization, thereby implying the potential involvement of phosphorylation in regulating the activities of the N protein at other levels including RNA-binding capacity.
Keywords
PRRSV; nucleocapsid protein; serine phosphoprotein; nuclear localization; homodimerization;
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