Cziepluch C, Lampel S, Grewenig A, Grund C, Lichter P, Rommelaere J
Applied Tumor Virology Unit, F0100 and Institut National de la Santé et de la Recherche Médicale U 375, Deutsches Krebsforschungszentrum, D-69120 Heidelberg, Germany.
J Virol. 2000 May;74(10):4807-15. doi: 10.1128/jvi.74.10.4807-4815.2000.
We have identified a nuclear structure that is induced after infection with the autonomous parvovirus H-1. Using fluorescence microscopy, we observed that the major nonstructural protein (NS1) of H-1 virus which is essential for viral DNA amplification colocalized with virus-specific DNA sequences and sites of ongoing viral DNA replication in distinct nuclear bodies which we designated H-1 parvovirus-associated replication bodies (H-1 PAR-bodies). In addition, two cellular proteins were shown to accumulate in H1 PAR-bodies: (i) the proliferating cell nuclear antigen (PCNA) which is essential for chromosomal and parvoviral replication and (ii) the NS1-interacting small glutamine-rich TPR-containing protein (SGT), suggesting a role for the latter in parvoviral replication and/or gene expression. Since many DNA viruses target preexisting nuclear structures, known as PML-bodies, for viral replication and gene expression, we have determined the localization of H-1 PAR- and PML-bodies by double-fluorescence labeling and confocal microscopy and found them to be spatially unrelated. Furthermore, H-1 PAR-bodies did not colocalize with other prominent nuclear structures such as nucleoli, coiled bodies, and speckled domains. Electron microscopy analysis revealed that NS1, as detected by indirect immunogold labeling, was localized in ring-shaped electron-dense nuclear structures corresponding in size and frequency to H-1 PAR-bodies. These structures were also clearly visible without immunogold labeling and could be detected only in infected cells. Our results suggest that H-1 virus does not target known nuclear bodies for DNA replication but rather induces the formation of a novel structure in the nucleus of infected cells.
我们鉴定出一种在自主细小病毒H-1感染后诱导形成的核结构。利用荧光显微镜,我们观察到H-1病毒的主要非结构蛋白(NS1)对于病毒DNA扩增至关重要,它与病毒特异性DNA序列以及正在进行病毒DNA复制的位点共定位于我们命名为H-1细小病毒相关复制体(H-1 PAR体)的独特核体中。此外,有两种细胞蛋白被证明在H1 PAR体中积累:(i)对染色体和细小病毒复制至关重要的增殖细胞核抗原(PCNA),以及(ii)与NS1相互作用的富含谷氨酰胺的含TPR小蛋白(SGT),这表明后者在细小病毒复制和/或基因表达中发挥作用。由于许多DNA病毒靶向预先存在的核结构(即PML体)进行病毒复制和基因表达,我们通过双荧光标记和共聚焦显微镜确定了H-1 PAR体和PML体的定位,发现它们在空间上没有关联。此外,H-1 PAR体与其他突出的核结构如核仁、卷曲体和斑点结构域没有共定位。电子显微镜分析显示,通过间接免疫金标记检测到的NS1定位于与H-1 PAR体大小和频率相对应的环形电子致密核结构中。这些结构在没有免疫金标记的情况下也清晰可见,并且仅在感染细胞中能检测到。我们的结果表明,H-1病毒不是靶向已知的核体进行DNA复制,而是在受感染细胞的细胞核中诱导形成一种新的结构。