Citation: CUN Wei, Jie CHEN, Ying ZHANG, Long-ding LIU, LI Qi-han. Analysis of the Cellular Localization of Herpes Simplex Virus 1 Immediate-early Protein ICP22 .VIROLOGICA SINICA, 2010, 25(3) : 158-167.  http://dx.doi.org/10.1007/s12250-010-3118-0

Analysis of the Cellular Localization of Herpes Simplex Virus 1 Immediate-early Protein ICP22

  • Corresponding author: LI Qi-han, imbcams.lq@gmail.com
  • Received Date: 11 November 2009
    Accepted Date: 08 March 2010
    Available online: 01 June 2010

    Fund Project: the Ph.D. Programs Foundation of Ministry of Education of China 20060023008The National Natural Science Foundation of China 30700028The National Natural Science Foundation of China 30670094

  • Nuclear proteins often form punctiform structures, but the precise mechanism for this process is unknown. As a preliminary study, we investigated the aggregation of an HSV-1 immediate-early protein, infected-cell protein 22 (ICP22), in the nucleus by observing the localization of ICP22-EGFP fusion protein. Results showed that, in high-level expression conditions, ICP22-EGFP gradually concentrates in the nucleus, persists throughout the cell cycle without disaggregation even in the cell division phase, and is finally distributed to daughter cells. We subsequently constructed a mammalian cell expression system, which had tetracycline- dependent transcriptional regulators. Consequently, the location of ICP22-EGFP in the nucleus changed with distinct induction conditions. This suggests that the cellular location of ICP22 is also influenced by promoter regulation, in addition to its own structure. Our findings provide new clues for the investigation of transcriptional regulation of viral genes. In addition, the non-protease reporter system we constructed could be utilized to evaluate the role of internal ribosome entry sites (IRES) on transcriptional regulation.

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    Analysis of the Cellular Localization of Herpes Simplex Virus 1 Immediate-early Protein ICP22

      Corresponding author: LI Qi-han, imbcams.lq@gmail.com
    • Institute of Medical Biology, Chinese Academy of Medical Sciences, Peking Union Medical College, Kunming 650118, China
    Fund Project:  the Ph.D. Programs Foundation of Ministry of Education of China 20060023008The National Natural Science Foundation of China 30700028The National Natural Science Foundation of China 30670094

    Abstract: Nuclear proteins often form punctiform structures, but the precise mechanism for this process is unknown. As a preliminary study, we investigated the aggregation of an HSV-1 immediate-early protein, infected-cell protein 22 (ICP22), in the nucleus by observing the localization of ICP22-EGFP fusion protein. Results showed that, in high-level expression conditions, ICP22-EGFP gradually concentrates in the nucleus, persists throughout the cell cycle without disaggregation even in the cell division phase, and is finally distributed to daughter cells. We subsequently constructed a mammalian cell expression system, which had tetracycline- dependent transcriptional regulators. Consequently, the location of ICP22-EGFP in the nucleus changed with distinct induction conditions. This suggests that the cellular location of ICP22 is also influenced by promoter regulation, in addition to its own structure. Our findings provide new clues for the investigation of transcriptional regulation of viral genes. In addition, the non-protease reporter system we constructed could be utilized to evaluate the role of internal ribosome entry sites (IRES) on transcriptional regulation.