Efficient interaction of the vesicular stomatitis virus P protein with the L protein or the N protein in cells expressing the recombinant proteins.
Efficient interaction of the vesicular stomatitis virus P protein with the L protein or the N protein in cells expressing the recombinant proteins.
复制标题
水疱性口炎病毒 P 蛋白与表达重组蛋白的细胞中的 L 蛋白或 N 蛋白的有效相互作用。
DOI：
10.1006/viro.1995.1219
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Banerjee,AK
中科院分区：
文献类型：
--
作者：
Takacs,AM;Banerjee,AK
Specific in vivo interaction between the phosphoprotein (P) and the large polymerase protein (L) from the Indiana serotype of vesicular stomatitis virus was studied using a two-hybrid system. Transfection of CHO cells with plasmids encoding GALPINDand VPINDfusion proteins resulted in an easily detectable level of CAT activity, indicating that PINDand LINDassociate in vivo in the absence of other viral proteins. Mutational studies of PINDdemonstrated that both domains I and II of PINDare important for PIND-LINDassociation. In addition, casein kinase II (CKII)-mediated phosphorylation within domain I of PINDwas necessary for efficient association with LIND. We have also used the two-hybrid system to show PINDinteraction with NINDin vivo . PINDand NINDassociated more strongly than PINDand LIND. A similiar strong association was observed in heterologous interaction studies between Indiana and New Jersey serotype P and N proteins. Mutational studies of PINDdemonstrated that, unlike what was found for PNJ-NNJassociation, only the C-terminal region of the P protein was important for efficient association with NIND. Like PNJ, CKII-mediated phosphorylation within domain I of PINDwas not required for PN association and, like NNJ, the C-terminal five amino acids of the NINDprotein were critical for P association with N. These results demonstrate the importance of phosphorylation and specific domains of the P protein in its interaction with the L and N proteins, which are necessary for viral transcription and replication, respectively.
