Khattar Sunil K, Yunus Abdul S, Samal Siba K
Virginia-Maryland Regional College of Veterinary Medicine, University of Maryland, College Park, MD 20742, USA1.
J Gen Virol. 2001 Apr;82(Pt 4):775-779. 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.
利用细胞内牛呼吸道合胞病毒（BRSV）-氯霉素乙酰转移酶（CAT）微型基因组复制系统，研究了牛呼吸道合胞病毒（BRSV）磷蛋白（P）与核衣壳（N）蛋白和大聚合酶（L）蛋白之间的相互作用。使用P特异性抗血清进行的共免疫沉淀试验表明，P蛋白可与N蛋白和L蛋白形成复合物。对P蛋白进行缺失突变分析，以确定P蛋白中与N蛋白和L蛋白相互作用的区域。结果表明，P蛋白上存在两个独立的N结合位点：一个位于161-180个氨基酸的内部区域，另一个位于221-241个氨基酸的C末端区域。L结合位点被定位到P蛋白包含121-160个氨基酸的区域。数据表明，P蛋白上的N蛋白和L蛋白结合域不重叠。
