Identification of regions of bovine respiratory syncytial virus N protein required for binding to P protein and self-assembly.
The interaction of bovine respiratory syncytial virus (BRSV) nucleocapsid protein (N) with itself and phosphoprotein (P) was investigated using the yeast two-hybrid system. N-P interaction was abolished by any of a series of internal deletions or deletions at the C terminus. In contrast, removal of up to 32 amino acids from the N terminus had little effect. Interestingly, while removal of the C-terminal 32 amino acids ablated interaction, it was largely restored by a second deletion removing up to 32 amino acids from the N terminus. Many of these interactions of the BRSV N protein demonstrated a pattern that was similar to those occurring in the N protein of related viruses. N-N interaction was abolished by any of the internal deletions; however, removal of up to 32 amino acids from the N terminus or C terminus was tolerated and increased the strength of the interaction between the two N proteins.
Krishnamurthy
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Virginia-Maryland Regional College of Veterinary Medicine, University of Maryland, College Park 20742, USA.
Samal
S K
SK
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D015707:HN Protein; D006367:HeLa Cells; D006801:Humans; D016296:Mutagenesis; D019251:Nucleocapsid / Q000235:genetics / Q000378:metabolism*; D018112:Respiratory Syncytial Virus, Bovine / Q000378:metabolism* / Q000502:physiology; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly
D015707:HN Protein; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C116204:attachment protein G