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Volume 23 Issue 3
June 2008

    Lei GUO, Ying ZHANG, Yan-chun CHE, Wen-juan WU, Wei-zhong LI, Li-chun WANG, Yun LIAO, Long-ding LIU and Qi-han LI. Interactions of the HSV-1 UL25 Capsid Protein with Cellular Microtubule-associated Protein[J]. Virologica Sinica, 2008, 23(3): 211-217. doi: 10.1007/s12250-008-2936-9
    Citation: Lei GUO, Ying ZHANG, Yan-chun CHE, Wen-juan WU, Wei-zhong LI, Li-chun WANG, Yun LIAO, Long-ding LIU, Qi-han LI. Interactions of the HSV-1 UL25 Capsid Protein with Cellular Microtubule-associated Protein .VIROLOGICA SINICA, 2008, 23(3) : 211-217.  http://dx.doi.org/10.1007/s12250-008-2936-9
    shu

    HSV-1核衣壳蛋白UL25与细胞内微管蛋白的相互作用及其生物化学分析

    cstr: 32224.14.s12250-008-2936-9

    • 中国医学科学院&北京协和医学院 医学生物学研究所

    • 通讯作者： 李琦涵*, qihanli@21cn.com
    • 收稿日期： 2008-01-18
      录用日期： 2008-02-22

    • 利用酵母双杂交筛选和半乳糖苷酶活性检测发现单纯疱疹病毒I型（HSV-1）核衣壳蛋白UL25与细胞骨架微管蛋白存在相互作用，对UL25蛋白细胞内荧光分析发现其定位于胞质中细胞骨架微管蛋白，进一步对其缺失突变体研究提示UL25蛋白在核内也发挥了功能。

      Abstract

      An interaction between the HSV-1 UL25 capsid protein and cellular microtubule-associated protein was found using a yeast two-hybrid screen and β–D-galactosidase activity assays. Immunofluorescence microscopy of the UL25 protein demonstrated its co-localization with cellular microtubule-associated protein in the plasma membrane. Further investigations with deletion mutants suggest that UL25 is likely to have a function in the nucleus.

    Interactions of the HSV-1 UL25 Capsid Protein with Cellular Microtubule-associated Protein

    • Institute of Medical Biology, Chinese Academy of Medical Sciences, Peking Union Medical College, Kunming 650118, China

    • Corresponding author: Qi-han LI, qihanli@21cn.com
    • Received Date: 18 January 2008
      Accepted Date: 22 February 2008

      Fund Project: National Natural Science Funds 30700028National Natural Science Funds 30670094National Natural Science Funds 30570081

    • An interaction between the HSV-1 UL25 capsid protein and cellular microtubule-associated protein was found using a yeast two-hybrid screen and β–D-galactosidase activity assays. Immunofluorescence microscopy of the UL25 protein demonstrated its co-localization with cellular microtubule-associated protein in the plasma membrane. Further investigations with deletion mutants suggest that UL25 is likely to have a function in the nucleus.
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      1. Ali M A, Forghani B, Cantin E M. 1996. Characteri-zation of an essential HSV-1 protein encoded by the UL25 gene reported to be involved in virus penetration and capsid assembly. Virology, 216 (1): 278-283.
          doi: 10.1006/viro.1996.0061

      2. Diefenbach R J, Miranda-Saksena M, Douglas M W, et al. 2008. Transport and egress of herpes simplex virus in neurons. Rev Med Virol, 18 (1): 35-51.
          doi: 10.1002/(ISSN)1099-1654

      3. Dohner K, Sodeik B. 2005. The role of the cytoskeleton during viral infection. Curr Top Microbiol Immunol, 285: 67-108.

      4. Dohner K, Wolfstein A, Prank U, et al. 2002. Function of dynein and dynactin in herpes simplex virus capsid transport type 1. Mol Biol Cell, 13 (8): 2795-2809.
          doi: 10.1091/mbc.01-07-0348

      5. Fuchs W, Klupp B G, Granzow H, et al. 2002. The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions. J Virol, 76 (1): 364-378.
          doi: 10.1128/JVI.76.1.364-378.2002

      6. Garner J A. 2003. Herpes simplex virion entry into and intracellular transport within mammalian cells. Adv Drug Deliv Rev, 55 (11): 1497-1513.
          doi: 10.1016/j.addr.2003.07.006

      7. Kaelin K, Dezelee S, Masse M J, et al. 2000. The UL25 protein of pseudorabies virus associates with capsids and localizes to the nucleus and to microtubules. J Virol, 74 (1): 474-482.
          doi: 10.1128/JVI.74.1.474-482.2000

      8. Klupp B G, Granzow H, Keil G M, et al. 2006. The capsid-associated UL25 protein of the alphaherpesvirus pseudorabies virus is nonessential for cleavage and encapsidation of genomic DNA but is required for nuclear egress of capsids. J Virol, 80 (13): 6235-6246.
          doi: 10.1128/JVI.02662-05

      9. Mcnab A R, Desai P, Person S, et al. 1998. The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA. J Virol, 72 (2): 1060-1070.

      10. Ogasawara M, Suzutani T, Yoshida I, et al. 2001. Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: Location of UL25 product in the capsid and demonstration that it binds DNA. J Virol, 75 (3): 1427-1436.
          doi: 10.1128/JVI.75.3.1427-1436.2001

      11. Ojala P M, Sodeik B, Ebersold M W, et al. 2000. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol Cell Biol, 20 (13): 4922-4931.
          doi: 10.1128/MCB.20.13.4922-4931.2000

      12. Reynolds A E, Wills E G, Roller R J, et al. 2002. Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J Virol, 76 (17): 8939-8952.
          doi: 10.1128/JVI.76.17.8939-8952.2002

      13. Sheaffer A K, Newcomb W W, Gao M, et al. 2001. Herpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to Its maturation. J Virol, 75 (2): 687-698.
          doi: 10.1128/JVI.75.2.687-698.2001

      14. Sodeik B, Ebersold M W, Helenius A. 1997. Microtubule mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J Cell Biol, 136 (5): 1007-1021.
          doi: 10.1083/jcb.136.5.1007

      15. Stow N D. 2001. Packaging of genomic and amplicon DNA by the herpes simplex virus type 1 UL25-null mutant KUL25NS. J Virol, 75 (22): 10755-10765.
          doi: 10.1128/JVI.75.22.10755-10765.2001

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      Interactions of the HSV-1 UL25 Capsid Protein with Cellular Microtubule-associated Protein

        Corresponding author: Qi-han LI, qihanli@21cn.com
      • Institute of Medical Biology, Chinese Academy of Medical Sciences, Peking Union Medical College, Kunming 650118, China
      • Received Date: 18 January 2008
      • Accepted Date: 22 February 2008
      Fund Project:  National Natural Science Funds 30700028National Natural Science Funds 30670094National Natural Science Funds 30570081

      Abstract: An interaction between the HSV-1 UL25 capsid protein and cellular microtubule-associated protein was found using a yeast two-hybrid screen and β–D-galactosidase activity assays. Immunofluorescence microscopy of the UL25 protein demonstrated its co-localization with cellular microtubule-associated protein in the plasma membrane. Further investigations with deletion mutants suggest that UL25 is likely to have a function in the nucleus.

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