Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1

Authors

  • Wan-Song Lin,

    1. Key Laboratory of Ministry of Education for Gastrointestinal Cancer, Research Center of Molecular Medicine, Fujian Medical University, Fuzhou City, China
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  • Bo-Yan Jiao,

    1. Key Laboratory of Ministry of Education for Gastrointestinal Cancer, Research Center of Molecular Medicine, Fujian Medical University, Fuzhou City, China
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  • Yun-Li Wu,

    1. Key Laboratory of Ministry of Education for Gastrointestinal Cancer, Research Center of Molecular Medicine, Fujian Medical University, Fuzhou City, China
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  • Wan-Nan Chen,

    1. Key Laboratory of Ministry of Education for Gastrointestinal Cancer, Research Center of Molecular Medicine, Fujian Medical University, Fuzhou City, China
    2. Key Laboratory of Tumor Microbiology, Department of Medical Microbiology, Fujian Medical University, Fuzhou City, China
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  • Prof. Xu Lin

    Corresponding author
    1. Key Laboratory of Ministry of Education for Gastrointestinal Cancer, Research Center of Molecular Medicine, Fujian Medical University, Fuzhou City, China
    2. Key Laboratory of Tumor Microbiology, Department of Medical Microbiology, Fujian Medical University, Fuzhou City, China
    • Key Laboratory of Ministry of Education for Gastrointestinal Cancer, Research Center of Molecular Medicine, Fujian Medical University, 88 Jiaotong Road, Fuzhou 350004, China.
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  • Wan-Song Lin and Bo-Yan Jiao contributed equally to this work.

  • None of the authors has a financial interest in this work.

Abstract

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. J. Med. Virol. 84:871–877, 2012. © 2012 Wiley Periodicals, Inc.

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