Journal of General Virology, Vol 79, 1399-1403, Copyright © 1998 by Society for General Microbiology

ARTICLES

Identification of regions of bovine respiratory syncytial virus N protein required for binding to P protein and self-assembly

S Krishnamurthy and SK Samal
Virginia-Maryland Regional College of Veterinary Medicine, University of Maryland, College Park 20742, USA.

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.

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