The role of nucleocapsid of HIV-1 in virus assembly
The role of nucleocapsid of HIV-1 in virus assembly
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DOI：
10.1006/viro.1998.9374
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发表时间：
1998-11-10
期刊：
影响因子：
3.7
通讯作者：
Yu, XF
中科院分区：
文献类型：
--
作者：
Dawson, L;Yu, XF
利用Gag截断突变体、核衣壳缺失突变体和Gag核衣壳区点突变体，在转染的COS细胞和稳定的t细胞系中研究了HIV-I Gag的核衣壳蛋白在病毒组装中的作用。与先前的研究一致，只包含Gag的基质和衣壳区域的截断不能有效地组装成颗粒；释放的颗粒状物质密度也比野生型hiv - 1轻。缺失p7核衣壳但含有c端p6蛋白的缺失突变体在颗粒释放方面也效率低下，释放的颗粒更轻，而只含有p7第一个锌指的缺失突变体可以更有效地组装成病毒粒子。这些结果清楚地表明p7对于病毒的组装和释放是不可或缺的。在n端基本结构域和两个锌指之间的基本连接区域的一些点突变，先前已被证明在体外降低了RNA结合[Schmalzbauer， E., Strack， B., Dannull， J., Guehmann， S., and Moelling， K.(1996)]。[j] .华北农学报，2009(2):1-7。一种由基质和衣壳组成的融合蛋白与已知具有非特异性RNA结合活性的异源病毒蛋白融合[Ribas， J. C., Fujimura， T., and Wickner， R. B.（1994）。化学，269:28420-28428]释放颗粒物质的效率略高于单独的基质和衣壳，并且这些颗粒的密度高于单独的基质和衣壳。这些结果证明了HIV-I核衣壳在病毒组装过程中的重要作用，并表明p7带正电的N端对这一作用至关重要。(C) 1998学术出版社。
The role of the nucleocapsid protein of HIV-I Gag in virus assembly was investigated using Gag truncation mutants, a nucleocapsid deletion mutant, and point mutations in the nucleocapsid region of Gag, in transfected COS cells, and in stable T-cell lines. Consistent with previous investigations, a truncation containing only the matrix and capsid regions of Gag was unable to assemble efficiently into particles; also, the pelletable material released was lighter than the density of wild-type HIV-I. A deletion mutant lacking p7 nucleocapsid but containing the C-terminal p6 protein was also inefficient in particle release and released lighter particles, while a truncation containing only the first zinc finger of p7 could assemble more efficiently into virions. These results clearly show that p7 is indispensable for virus assembly and release. Some point mutations in the N-terminal basic domain and in the basic linker region between the two zinc fingers, which had been previously shown to have reduced RNA binding in vitro [Schmalzbauer, E., Strack, B., Dannull, J., Guehmann, S., and Moelling, K. (1996). J. Virol. 70: 771-777], were shown to reduce virus assembly dramatically when expressed in full-length viral clones. A fusion protein consisting of matrix and capsid fused to a heterologous viral protein known to have nonspecific RNA binding activity [Ribas, J. C., Fujimura, T., and Wickner, R. B. (1994) J. Biol. Chem. 269: 28420-28428] released pelletable material slightly more efficiently than matrix and capsid alone, and these particles had density higher than matrix and capsid alone. These results demonstrate the essential role of HIV-I nucleocapsid in the virus assembly process and show that the positively charged N terminus of p7 is critical for this role. (C) 1998 Academic Press.