Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N-P and P-L interactions using a minigenome system

• Published in: Journal of general virology Vol. 82; no. 4; pp. 775 - 779
• Main Authors: Khattar, S.K, Yunus, A.S, Samal, S.K
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01.04.2001
• Subjects: AL protein; amino acids; AN protein; antiserum; AP protein; binding proteins; Binding Sites; Bovine respiratory syncytial virus; Genome, Viral; mutants; nucleocapsid; Nucleocapsid - chemistry; Nucleocapsid - metabolism; phosphoproteins; Phosphoproteins - chemistry; Phosphoproteins - metabolism; protein binding; Respiratory Syncytial Virus, Bovine - chemistry; Respiratory Syncytial Virus, Bovine - genetics; Viral Proteins - chemistry; Viral Proteins - metabolism
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-82-4-775

The interaction of bovine respiratory syncytial virus (BRSV) phosphoprotein (P) with nucleocapsid (N) and large polymerase (L) proteins was investigated using an intracellular BRSV-CAT minigenome replication system. Coimmunoprecipitation assays using P-specific antiserum revealed that the P protein can form complexes with N and L proteins. Deletion mutant analysis of the P protein was performed to identify the regions of P protein that interact with N and L proteins. The results indicate that two independent N-binding sites exist on the P protein: an internal region of 161-180 amino acids and a C-terminal region of 221-241 amino acids. The L-binding site was mapped to a region of P protein encompassing amino acids 121-160. The data suggest that N and L protein binding domains on the P protein do not overlap.