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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 [J].VIROLOGICA SINICA, 2008, 23(3) : 211-217.  http://dx.doi.org/10.1007/s12250-008-2936-9

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

  • Corresponding author: Qi-han LI, qihanli@21cn.com
  • Received Date: 18 January 2008
    Accepted Date: 22 February 2008
    Available online: 01 June 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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    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.
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    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.
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    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.
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    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.
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    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.
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    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
    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.