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

被引:16
作者
Krishnamurthy, S [1 ]
Samal, SK [1 ]
机构
[1] Univ Maryland, Virginia Maryland Reg Coll Vet Med, College Pk, MD 20742 USA
关键词
D O I
10.1099/0022-1317-79-6-1399
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:1399 / 1403
页数:5
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