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狂犬病病毒磷蛋白(P)与核蛋白(N)的体内相互作用:P蛋白上存在两个N结合位点。

In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein.

作者信息

Chenik M, Chebli K, Gaudin Y, Blondel D

机构信息

Laboratoire de Génétique des Virus, CNRS, Gif sur Yvette, France.

出版信息

J Gen Virol. 1994 Nov;75 ( Pt 11):2889-96. doi: 10.1099/0022-1317-75-11-2889.

Abstract

The rabies virus phosphoprotein (P) and nucleoprotein (N) are involved in transcription and replication of the viral genome. Interaction between N and P was studied in vivo in transfected cells expressing both proteins. Co-immunoprecipitation assays revealed that the N-P complex is present in cells expressing both proteins as well as in infected cells. Furthermore, immunostaining showed that coexpression of N and P was sufficient to induce the formation of cytoplasmic inclusions similar to those found in infected cells. In addition, deletion mutant analysis of P was performed to identify the regions of P interacting with N. The results indicate that at least two independent N-binding sites exist on P protein: one is located in the carboxy-terminal part of the protein and another between amino acids 69 and 177. The formation of cytoplasmic inclusions seems to require the presence of both N-binding sites on P protein.

摘要

狂犬病病毒磷蛋白(P)和核蛋白(N)参与病毒基因组的转录和复制。在同时表达这两种蛋白的转染细胞中对N和P之间的相互作用进行了体内研究。免疫共沉淀分析表明,N-P复合物存在于同时表达这两种蛋白的细胞以及受感染细胞中。此外,免疫染色显示,N和P的共表达足以诱导形成与受感染细胞中发现的类似的细胞质内含物。另外,对P进行了缺失突变分析以确定P与N相互作用的区域。结果表明,P蛋白上至少存在两个独立的N结合位点:一个位于该蛋白的羧基末端部分,另一个位于氨基酸69和177之间。细胞质内含物的形成似乎需要P蛋白上两个N结合位点的存在。

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