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) nucleocap sid protein (N) with itself and phosphoprotein (P) was investigated us ing 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 litt le effect. Interestingly, while removal of the C-terminal 32 amino aci ds ablated interaction, it was largely restored by a second deletion r emoving up to 32 amino acids from the N terminus. Many of these intera ctions of the BRSV N protein demonstrated a pattern that was similar t o those occurring in the N protein of related viruses. N-N interaction was abolished by any of the internal deletions; however, removal of u p to 32 amino acids from the N terminus or C terminus was tolerated an d increased the strength of the interaction between the two N proteins .