Archives of Virology

, Volume 154, Issue 3, pp 519–524 | Cite as

Role of glyceraldehyde-3-phosphate dehydrogenase binding to hepatitis B virus posttranscriptional regulatory element in regulating expression of HBV surface antigen

  • Yi Li
  • Tingting Huang
  • Xiaohua Zhang
  • Tao Wan
  • Jieli Hu
  • Ailong Huang
  • Hua Tang
Brief Report

Abstract

The hepatitis B virus (HBV) posttranscriptional regulatory element (HPRE) has been demonstrated to facilitate the cytoplasmic localization of unspliced transcripts. One cellular protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), is known to combine with this element. However, its function on HPRE remains unclear. Here, we show that recombinant GAPDH protein binds to HPRE RNA in vitro in streptavidin pull-down assays. Functional analysis demonstrated that GAPDH inhibited HPRE function in a pDM138-HPRE chloramphenicol acetyltransferase reporter assay system. Overexpression of GAPDH depressed the expression of HBs antigen, as detected both in cells transiently expressing HBs-HPRE and in HepG2.2.15 cells. These data indicate that GAPDH may be involved in the posttranscriptional regulation of HBV, which is critical for the life cycle of HBV.

Notes

Acknowledgments

We thank Yen, T. S. B. for providing us pDM138 and pDM138-HPRE plasmids. This work was supported by Nature Science Foundation of China (30771924).

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Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Yi Li
    • 1
  • Tingting Huang
    • 1
  • Xiaohua Zhang
    • 1
  • Tao Wan
    • 1
  • Jieli Hu
    • 1
  • Ailong Huang
    • 1
  • Hua Tang
    • 1
  1. 1.Key Laboratory of Molecular Infectious Diseases, Ministry of EducationChongqing Medical UniversityChongqingChina

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