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VA-MD Regional College of Veterinary Medicine, University of Maryland, College Park, MD 20742, USA
Specific interactions between the nucleocapsid protein (N) and the phosphoprotein (P) of bovine respiratory syncytial virus (BRSV) have been investigated using a yeast-based two-hybrid system. Plasmids encoding the yeast GAL4 DNA binding domain fused with the N gene and GAL4 activation domain fused with the P gene were cotransfected into competent yeast cells. The ability of the N and P proteins to interact in vivo was measured by activation of the lacZ reporter gene by the GAL4 transactivation region. Results indicated that the N and P proteins interact very strongly in vivo. When interactions between N and various deletion mutants of the P protein were examined, an internal region (aa 132–168) and the highly acidic C-terminal region (aa 236–241) of the P protein were found to be essential for N-P interaction. In addition, the highly basic N-terminal region (amino acids 1–40) was found to be involved in N-P interaction to a lesser extent.
* Author for correspondence. Fax +1 301 935 6079. e-mail SS5@umail.umd.edu
Present address: Laboratory of Clinical Investigation, NIAID, National Institutes of Health, Bethesda, MD 20892, USA.
Present address: Insect Neurobiology and Hormone Laboratory, USDA, ARS, Beltsville, MD 20705, USA.
Received 11 September 1995;
accepted 19 December 1995.
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