重组流感病毒核糖核蛋白的超微结构和功能分析表明，在病毒扩增过程中核蛋白会发生二聚化。
Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification.
作者信息
Ortega J, Martín-Benito J, Zürcher T, Valpuesta J M, Carrascosa J L, Ortín J
机构信息
Centro Nacional de Biotecnología (CSIC), Campus de Cantoblanco, 28049 Madrid, Spain.
出版信息
J Virol. 2000 Jan;74(1):156-63. doi: 10.1128/jvi.74.1.156-163.2000.
Abstract
Influenza virus ribonucleoproteins (RNPs) were reconstituted in vivo from cloned cDNAs expressing the three polymerase subunits, the nucleoprotein (NP), and short template RNAs. The structure of purified RNPs was studied by electron microscopy and image processing. Circular and elliptic structures were obtained in which the NP and the polymerase complex could be defined. Comparison of the structure of RNPs of various lengths indicated that each NP monomer interacts with approximately 24 nucleotides. The analysis of the amplification of RNPs with different lengths showed that those with the highest replication efficiency contained an even number of NP monomers, suggesting that the NP is incorporated as dimers into newly synthesized RNPs.
摘要
流感病毒核糖核蛋白（RNP）在体内由表达三种聚合酶亚基、核蛋白（NP）和短模板RNA的克隆cDNA重组而成。通过电子显微镜和图像处理研究了纯化的RNP的结构。获得了圆形和椭圆形结构，其中NP和聚合酶复合物可以被确定。对不同长度RNP结构的比较表明，每个NP单体与大约24个核苷酸相互作用。对不同长度RNP扩增的分析表明，复制效率最高的那些RNP含有偶数个NP单体，这表明NP以二聚体形式掺入新合成的RNP中。
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