Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N-P interaction using a two-hybrid system

The Journal of General Virology
S K MallipeddiS K Samal

Abstract

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.

Citations

Apr 16, 2004·Clinical Microbiology Reviews·Andrew J EastonHelene F Rosenberg
Oct 8, 2014·Proceedings of the National Academy of Sciences of the United States of America·Robert CoxMing Luo
Jan 17, 2014·Journal of Virology·Todd J GreenMing Luo
Jan 30, 2007·Veterinary Research·Jean-Francois Valarcher, Geraldine Taylor
Jan 19, 2020·Nature Communications·Dongdong CaoBo Liang

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