Two hnRNP-associated proteins share common structural features with the adenoviral 72-kDa protein.
Two hnRNP-associated proteins share common structural features with the adenoviral 72-kDa protein.
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两种 hnRNP 相关蛋白与腺病毒 72-kDa 蛋白具有共同的结构特征。
DOI：
10.1006/excr.1995.1001
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发表时间：
1995
影响因子：
3.7
通讯作者：
J. Fuchs
中科院分区：
文献类型：
--
作者：
D. Mahé;R. Roussev;Y. Lutz;F. Puvion;J. Fuchs
利用我们的抗hnRNP单克隆抗体库Y.卢茨，M。雅各布和J P. Fuchs（1988）Exp.小区资源：175，108-124; P. Mähl，Y.卢茨，E. Puvion和J. - P. Fuchs，（1989）J. Cell Biol.109，1921-1935，我们通过免疫细胞荧光研究了HeLa细胞被2型腺病毒感染后一系列斑点状分布的核抗原的命运。虽然斑点图案，这对应于核质fibrillogranular网络，包括间染色质颗粒簇，仍然观察到在大多数的感染周期，几种抗体也揭示了额外的，越来越荧光病毒诱导的结构。在未感染的细胞中，这些抗体中的两种，称为3F 2和2A 5，分别识别33和31 kDa的两种抗原。Western印迹分析表明，在感染细胞中观察到的荧光量增加并不反映33-和31-kDa抗原的积累，但实际上是由于两种抗体也识别多功能腺病毒72-kDa单链DNA结合蛋白（DBP）的事实。免疫电子显微镜分析，包括连续的双标记，确实表明，这种额外的信号精确地与病毒的72-kDa的DBP，它基本上积累在整个表面的病毒诱导的单链DNA积累位点共定位。两者合计，我们的数据表明，两个主机特异性hnRNP相关抗原与病毒72 kDa DBP共享共同的表位。
Using our anti-hnRNP monoclonal antibody library Y. Lutz, M. Jacob, and J.-P. Fuchs (1988) Exp. Cell Res., 175, 108-124; P. Mähl, Y. Lutz, E. Puvion, and J.-P. Fuchs, (1989) J. Cell Biol. 109, 1921-1935, we investigated by immunocytofluorescence the fate of a series of speckled-distributed nuclear antigens, after HeLa cells were infected with adenovirus type 2. Although the speckled pattern, which corresponds to the nucleoplasmic fibrillogranular network, including the interchromatin-granule clusters, was still observed during most of the infectious cycle, several antibodies also revealed additional, increasingly fluorescent virus-induced structures. In noninfected cells, two of these antibodies, termed 3F2 and 2A5, recognize two antigens of 33 and 31 kDa, respectively. Western blot analysis showed that this increasing amount of fluorescence observed in infected cells did not reflect an accumulation of the 33- and 31-kDa antigens, but is actually due to the fact that both antibodies also recognize the multifunctional adenovirus 72-kDa single-stranded DNA-binding protein (DBP). Immunoelectron microscopy analyses, including sequential double-labeling, indeed showed that this additional signal precisely colocalizes with the viral 72-kDa DBP, which essentially accumulates over the entire surface of the virus-induced single-stranded DNA accumulation sites. Taken together, our data show that two host-specific hnRNP-associated antigens share common epitopes with the viral 72-kDa DBP.