Glyceraldehyde 3-phosphate dehydrogenase negatively regulates human immunodeficiency virus type 1 infection

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• 作者：Naoki Kishimoto (1)
  Ayano Onitsuka (1)
  Keishi Kido (1)
  Nobutoki Takamune (1)
  Shozo Shoji (1) (2)
  Shogo Misumi (1)
  
• 关键词：Glyceraldehyde 3 ; phosphate dehydrogenase ; Lysyl ; tRNA synthetase ; tRNALys3 ; Human immunodeficiency virus type 1
• 刊名：Retrovirology
• 出版年：2012
• 出版时间：December 2012
• 年：2012
• 卷：9
• 期：1
• 全文大小：487KB
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• 作者单位：Naoki Kishimoto (1)
  Ayano Onitsuka (1)
  Keishi Kido (1)
  Nobutoki Takamune (1)
  Shozo Shoji (1) (2)
  Shogo Misumi (1)
  
  1. Department of Pharmaceutical Biochemistry, Faculty of Medical and Pharmaceutical Sciences, Kumamoto University, Kumamoto, 862-0973, Japan
  2. Kumamoto Health Science University, Kumamoto, 861-5598, Japan
  
• ISSN：1742-4690

文摘

Background Host proteins are incorporated inside human immunodeficiency virus type 1 (HIV-1) virions during assembly and can either positively or negatively regulate HIV-1 infection. Although the identification efficiency of host proteins is improved by mass spectrometry, how those host proteins affect HIV-1 replication has not yet been fully clarified. Results In this study, we show that virion-associated glyceraldehyde 3-phosphate dehydrogenase (GAPDH) does not allosterically inactivate HIV-1 reverse transcriptase (RT) but decreases the efficiency of reverse transcription reactions by decreasing the packaging efficiency of lysyl-tRNA synthetase (LysRS) and tRNALys3 into HIV-1 virions. Two-dimensional (2D) gel electrophoresis demonstrated that some isozymes of GAPDH with different isoelectric points were expressed in HIV-1-producing CEM/LAV-1 cells, and a proportion of GAPDH was selectively incorporated into the virions. Suppression of GAPDH expression by RNA interference in CEM/LAV-1 cells resulted in decreased GAPDH packaging inside the virions, and the GAPDH-packaging-defective virus maintained at least control levels of viral production but increased the infectivity. Quantitative analysis of reverse transcription products indicated that the levels of early cDNA products of the GAPDH-packaging-defective virus were higher than those of the control virus owing to the higher packaging efficiencies of LysRS and tRNALys3 into the virions rather than the GAPDH-dependent negative allosteric modulation for RT. Furthermore, immunoprecipitation assay using an anti-GAPDH antibody showed that GAPDH directly interacted with Pr55 gag and p160 gag-pol and the overexpression of LysRS in HIV-1-producing cells resulted in a decrease in the efficiency of GAPDH packaging in HIV particles. In contrast, the viruses produced from cells expressing a high level of GAPDH showed decreased infectivity in TZM-bl cells and reverse transcription efficiency in TZM-bl cells and peripheral blood mononuclear cells (PBMCs). Conclusions These findings indicate that GAPDH negatively regulates HIV-1 infection and provide insights into a novel function of GAPDH in the HIV-1 life cycle and a new host defense mechanism against HIV-1 infection.