|Fernandez-Sainz, Ignacio - USDA, ARS ORISE FELLOW|
|Lu, Zhiqiang - US DHS, S&T, PIADC|
Submitted to: American Society for Virology Meeting
Publication Type: Abstract Only
Publication Acceptance Date: June 3, 2009
Publication Date: July 10, 2009
Citation: Gladue, D.P., Holinka-Patterson, L.G., Fernandez-Sainz, I., Prarat, M.V., Lu, Z., Borca, M.V. 2009. Sumoylation of the Core Protein in Classical Swine Fever Virus is Essential for Virulence in swine. American Society for Virology Meeting. Paper No. W49-5: P. 213. Technical Abstract: The classical swine fever virus core protein makes up the nucleocapsid of the virus, and is serves both as a protective function for the viral RNA and a transcriptional regulator in the host cell. To identify host proteins that interact with the viral Core protein we utilized the yeast two-hybrid to screen against a swine macrophage cDNA library. Several proteins were specific binding partners of the core protein. Two proteins identified are involved in the sumoylation pathway, SUMO1 (small ubiquitin-like modifier) and UBC9 (ubiquitin-like protein SUMO1 conjugating enzyme). Sumoylation is a reversible post-translational modification that has been shown to have various effects on its protein targets, such as to modulate the function of several transcription factors. Protein modification by SUMO1 occurs by covalently binding to specific lysine residues in the target protein. In the CSFV core protein there are twenty-one lysines (K) that are possible sites for sumoylation. We mutated and characterized five lysines with the highest probability of being modified by SUMO1. We determined sumoylation residues critical for SUMO1 recognition and essential for viral virulence in swine.