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Volume 25 Issue 1
February 2010
    Citation: Fu-sen LIN, Qiong DING, Hong GUO, Alan C. ZHENG. The Herpes Simplex Virus Type 1 Infected Cell Protein 22 .VIROLOGICA SINICA, 2010, 25(1) : 1-7.  http://dx.doi.org/10.1007/s12250-010-3080-x
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    The Herpes Simplex Virus Type 1 Infected Cell Protein 22

    cstr: 32224.14.s12250-010-3080-x

    • State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China

    • Corresponding author: Alan C. ZHENG, zhengcf@wh.iov.cn
    • Equal contribution author
    • Received Date: 31 May 2009
      Accepted Date: 16 July 2009
      Available online: 01 February 2010

      Fund Project: Open Research Fund Program of the State Key Laboratory of Virology of China 2009007the Hundred Talents Program of the Chinese Academy of Science 20071010-141Hubei Province Natural Science Foundation of Innovation Groups Project 2008CDA013National Natural Science Foundation of China 30870120Open Research Fund Program of the State Key Laboratory of Virology of China 2007003

    • As one of the immediate-early (IE) proteins of herpes simplex virus type 1 (HSV-1), ICP22 is a multifunctional viral regulator that localizes in the nucleus of infected cells. It is required in experimental animal systems and some nonhuman cell lines, but not in Vero or HEp-2 cells. ICP22 is extensively phosphorylated by viral and cellular kinases and nucleotidylylated by casein kinase II. It has been shown to be required for efficient expression of early (E) genes and a subset of late (L) genes. ICP22, in conjunction with the UL13 kinase, mediates the phosphorylation of RNA polymerase II. Both ICP22 and UL13 are required for the activation of cdc2, the degradation of cyclins A and B and the acquisition of a new cdc2 partner, the UL42 DNA polymerase processivity factor. The cdc2–UL42 complex mediates postranscriptional modification of topoisomerase IIα in an ICP22-dependent manner to promote L gene expression. In addition, ICP22 interacts with cdk9 in a Us3 kinase dependent fashion to phosphorylate RNA polymerase II.
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      42. Ward P L, Taddeo B, Markovitz N S, et al. 2000. Identification of a novel expressed open reading frame situated between genes U(L)20 and U(L)21 of the herpes simplex virus 1 genome. Virology, 266 (2): 275-285.
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      The Herpes Simplex Virus Type 1 Infected Cell Protein 22

        Corresponding author: Alan C. ZHENG, zhengcf@wh.iov.cn
      • State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China
      • Received Date: 31 May 2009
      • Accepted Date: 16 July 2009
      Fund Project:  Open Research Fund Program of the State Key Laboratory of Virology of China 2009007the Hundred Talents Program of the Chinese Academy of Science 20071010-141Hubei Province Natural Science Foundation of Innovation Groups Project 2008CDA013National Natural Science Foundation of China 30870120Open Research Fund Program of the State Key Laboratory of Virology of China 2007003

      Abstract: As one of the immediate-early (IE) proteins of herpes simplex virus type 1 (HSV-1), ICP22 is a multifunctional viral regulator that localizes in the nucleus of infected cells. It is required in experimental animal systems and some nonhuman cell lines, but not in Vero or HEp-2 cells. ICP22 is extensively phosphorylated by viral and cellular kinases and nucleotidylylated by casein kinase II. It has been shown to be required for efficient expression of early (E) genes and a subset of late (L) genes. ICP22, in conjunction with the UL13 kinase, mediates the phosphorylation of RNA polymerase II. Both ICP22 and UL13 are required for the activation of cdc2, the degradation of cyclins A and B and the acquisition of a new cdc2 partner, the UL42 DNA polymerase processivity factor. The cdc2–UL42 complex mediates postranscriptional modification of topoisomerase IIα in an ICP22-dependent manner to promote L gene expression. In addition, ICP22 interacts with cdk9 in a Us3 kinase dependent fashion to phosphorylate RNA polymerase II.

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