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首页> 外文期刊>Journal of Medical Virology >Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1
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Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1

机译:乙型肝炎病毒X蛋白通过与真核翻译Elongat离子因子1α1的相互作用阻断丝状肌动蛋白束

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摘要

Hepatitis B virus (HBV)-encoded X protein (HBx protein) is a multi-functional regulatory protein. It functions by protein-protein interaction and plays a pivotal role in the pathogenesis of HBV-related diseases. However, the partners in hepatocytes interacting with HBx protein are far from understood fully. In this study, immunoprecipitation was employed to screen for binding partners for the HBx protein from huh-7 hepatoma cells infected with recombinant adenovirus expressing HBx protein, and five cellular proteins including eukaryotic translation elongation factor 1 alpha 1 (eEF1A1), were identified. The interaction between HBx protein and eEF1A1 was confirmed further using a GST pull-down assay and co-immunoprecipitation, respectively. In Huh-7 hepatoma cells, the HBx protein inhibits dimer formation of eEF1A1, hence blocks filamentous actin bundling. These findings provide new insights into the molecular mechanisms involved in the functions of the HBx protein.
机译:乙型肝炎病毒(HBV) - 索尼酸X蛋白(HBX蛋白)是一种多功能调节蛋白。 它通过蛋白质 - 蛋白质相互作用起作用,并在HBV相关疾病的发病机制中发挥枢轴作用。 然而,与HBX蛋白相互作用的肝细胞中的伴侣远非完全理解。 在该研究中,使用免疫沉淀到来自Huh-7 HBX蛋白的HBX蛋白的结合伴侣,其来自表达HBX蛋白的重组腺病毒的HUH-7肝癌细胞,并且鉴定了包括真核转化伸长因子1(EEF1A1)的五种细胞蛋白质。 使用GST下拉测定和共免疫沉淀,进一步确认HBX蛋白和EEF1A1之间的相互作用。 在HUH-7肝癌细胞中,HBX蛋白抑制EEF1A1的二聚体形成,因此阻断丝状肌动蛋白捆扎。 这些发现提供了新的见解,进入HBX蛋白的功能的分子机制。

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