Abstract
Herpes simplex virus type 1 (HSV-1) is a common human pathogen causing cold sores and even more serious diseases. It can establish a latent stage in sensory ganglia after primary epithelial infections, and reactivate in response to stress or sunlight. Previous studies have demonstrated that viral immediate-early protein ICP0 plays a key role in regulating the balance between lytic and latent infection. Recently, It has been determined that promyelocytic leukemia (PML) nuclear bodies (NBs), small nuclear sub-structures, contribute to the repression of HSV-1 infection in the absence of functional ICP0. In this review, we discuss the fundamentals of the interaction between ICP0 and PML NBs, suggesting a potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1.
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Ahn, J.H., and Hayward, G.S. (2000). Disruption of PML-associated nuclear bodies by IE1 correlates with efficient early stages of viral gene expression and DNA replication in human cytomegalovirus infection. Virology 274, 39–55.
Antón, L.C., Schubert, U., Bacík, I., Princiotta, M.F., Wearsch, P.A., Gibbs, J., Day, P.M., Realini, C., Rechsteiner, M.C., Bennink, J.R., et al. (1999). Intracellular localization of proteasomal degradation of a viral antigen. J Cell Biol 146, 113–124.
Aslani, A., Simonsson, S., and Elias, P. (2000). A novel conformation of the herpes simplex virus origin of DNA replication recognized by the origin binding protein. J Biol Chem 275, 5880–5887.
Bell, P., Lieberman, P.M., and Maul, G.G. (2000). Lytic but not latent replication of epstein-barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins. J Virol 74, 11800–11810.
Bernardi, R., and Pandolfi, P.P. (2003). Role of PML and the PML-nuclear body in the control of programmed cell death. Oncogene 22, 9048–9057.
Bischof, O., Kirsh, O., Pearson, M., Itahana, K., Pelicci, P.G., and Dejean, A. (2002). Deconstructing PML-induced premature senescence. EMBO J 21, 3358–3369.
Blondel, D., Kheddache, S., Lahaye, X., Dianoux, L., and Chelbi-Alix, M.K. (2010). Resistance to rabies virus infection conferred by the PMLIV isoform. J Virol 84, 10719–10726.
Blondel, D., Regad, T., Poisson, N., Pavie, B., Harper, F., Pandolfi, P.P., De Thé, H., and Chelbi-Alix, M.K. (2002). Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies. Oncogene 21, 7957–7970.
Bonilla, W.V., Pinschewer, D.D., Klenerman, P., Rousson, V., Gaboli, M., Pandolfi, P.P., Zinkernagel, R.M., Salvato, M.S., and Hengartner, H. (2002). Effects of promyelocytic leukemia protein on virus-host balance. J Virol 76, 3810–3818.
Boutell, C., and Everett, R.D. (2003). The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and Ubiquitinates p53. J Biol Chem 278, 36596–36602.
Boutell, C., Sadis, S., and Everett, R.D. (2002). Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro. J Virol 76, 841–850.
Cai, W., Astor, T.L., Liptak, L.M., Cho, C., Coen, D.M., and Schaffer, P.A. (1993). The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency. J Virol 67, 7501–7512.
Cai, W., and Schaffer, P.A. (1991). A cellular function can enhance gene expression and plating efficiency of a mutant defective in the gene for ICP0, a transactivating protein of herpes simplex virus type 1. J Virol 65, 4078–4090.
Cai, W., and Schaffer, P.A. (1992). Herpes simplex virus type 1 ICP0 regulates expression of immediate-early, early, and late genes in productively infected cells. J Virol 66, 2904–2915.
Chelbi-Alix, M.K., and de Thé, H. (1999). Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18, 935–941.
Chelbi-Alix, M.K., Quignon, F., Pelicano, L., Koken, M.H., and de Thé, H. (1998). Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J Virol 72, 1043–1051.
Cuchet-Lourenço, D., Boutell, C., Lukashchuk, V., Grant, K., Sykes, A., Murray, J., Orr, A., and Everett, R.D. (2011). SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes. PLoS Pathog 7, e1002123.
Dellaire, G., and Bazett-Jones, D.P. (2004). PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26, 963–977.
Dellaire, G., Ching, R.W., Ahmed, K., Jalali, F., Tse, K.C., Bristow, R.G., and Bazett-Jones, D.P. (2006). Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR. J Cell Biol 175, 55–66.
DeLuca, N.A., McCarthy, A.M., and Schaffer, P.A. (1985). Isolation and characterization of deletion mutants of herpes simplex virus type 1 in the gene encoding immediate-early regulatory protein ICP4. J Virol 56, 558–570.
Doucas, V., Ishov, A.M., Romo, A., Juguilon, H., Weitzman, M.D., Evans, R.M., and Maul, G.G. (1996). Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev 10, 196–207.
Duprez, E., Saurin, A.J., Desterro, J.M., Lallemand-Breitenbach, V., Howe, K., Boddy, M.N., Solomon, E., de Thé, H., Hay, R.T., and Freemont, P.S. (1999). SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J Cell Sci 112, 381–393.
Efstathiou, S., and Preston, C.M. (2005). Towards an understanding of the molecular basis of herpes simplex virus latency. Virus Res 111, 108–119.
El McHichi, B., Regad, T., Maroui, M.A., Rodriguez, M.S., Aminev, A., Gerbaud, S., Escriou, N., Dianoux, L., and Chelbi-Alix, M.K. (2010). SUMOylation promotes PML degradation during encephalomyocarditis virus infection. J Virol 84, 11634–11645.
Everett, R.D. (1988). Analysis of the functional domains of herpes simplex virus type 1 immediate-early polypeptide Vmw110. J Mol Biol 202, 87–96.
Everett, R.D. (1989). Construction and characterization of herpes simplex virus type 1 mutants with defined lesions in immediate early gene 1. J Gen Virol 70, 1185–1202.
Everett, R.D. (2000). ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioessays 22, 761–770.
Everett, R.D. (2001). DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20, 7266–7273.
Everett, R.D. (2006). Interactions between DNA viruses, ND10 and the DNA damage response. Cell Microbiol 8, 365–374.
Everett, R.D., Boutell, C., and Orr, A. (2004a). Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0. J Virol 78, 1763–1774.
Everett, R.D., and Chelbi-Alix, M.K. (2007). PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89, 819–830.
Everett, R.D., Earnshaw, W.C., Findlay, J., and Lomonte, P. (1999a). Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J 18, 1526–1538.
Everett, R.D., Freemont, P., Saitoh, H., Dasso, M., Orr, A., Kathoria, M., and Parkinson, J. (1998a). The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J Virol 72, 6581–6591.
Everett, R.D., Lomonte, P., Sternsdorf, T., van Driel, R., and Orr, A. (1999b). Cell cycle regulation of PML modification and ND10 composition. J Cell Sci 112, 4581–4588.
Everett, R.D., and Maul, G.G. (1994). HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J 13, 5062–5069.
Everett, R.D., Meredith, M., Orr, A., Cross, A., Kathoria, M., and Parkinson, J. (1997). A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J 16, 566–577.
Everett, R.D., and Murray, J. (2005). ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J Virol 79, 5078–5089.
Everett, R.D., Murray, J., Orr, A., and Preston, C.M. (2007). Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts. J Virol 81, 10991–11004.
Everett, R.D., Orr, A., and Preston, C.M. (1998b). A viral activator of gene expression functions via the ubiquitin-proteasome pathway. EMBO J 17, 7161–7169.
Everett, R.D., Parada, C., Gripon, P., Sirma, H., and Orr, A. (2008a). Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J Virol 82, 2661–2672.
Everett, R.D., Rechter, S., Papior, P., Tavalai, N., Stamminger, T., and Orr, A. (2006). PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J Virol 80, 7995–8005.
Everett, R.D., Sourvinos, G., Leiper, C., Clements, J.B., and Orr, A. (2004b). Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes. J Virol 78, 1903–1917.
Everett, R.D., Young, D.F., Randall, R.E., and Orr, A. (2008b). STAT-1- and IRF-3-dependent pathways are not essential for repression of ICP0-null mutant herpes simplex virus type 1 in human fibroblasts. J Virol 82, 8871–8881.
Ferenczy, M.W., and DeLuca, N.A. (2011). Reversal of heterochromatic silencing of quiescent herpes simplex virus type 1 by ICP0. J Virol 85, 3424–3435.
Fraefel, C., Bittermann, A.G., Büeler, H., Heid, I., Bächi, T., and Ackermann, M. (2004). Spatial and temporal organization of adeno-associated virus DNA replication in live cells. J Virol 78, 389–398.
Fukuyo, Y., Horikoshi, N., Ishov, A.M., Silverstein, S.J., and Nakajima, T. (2011). The herpes simplex virus immediate-early ubiquitin ligase ICP0 induces degradation of the ICP0 repressor protein E2FBP1. J Virol 85, 3356–3366.
Fukuyo, Y., Mogi, K., Tsunematsu, Y., and Nakajima, T. (2004). E2FBP1/hDril1 modulates cell growth through downregulation of promyelocytic leukemia bodies. Cell Death Differ 11, 747–759.
Gresko, E., Ritterhoff, S., Sevilla-Perez, J., Roscic, A., Fröbius, K., Kotevic, I., Vichalkovski, A., Hess, D., Hemmings, B.A., and Schmitz, M.L. (2009). PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage. Oncogene 28, 698–708.
Gu, H., and Roizman, B. (2003). The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proc Natl Acad Sci U S A 100, 8963–8968.
Hagglund, R., and Roizman, B. (2002). Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0. Proc Natl Acad Sci U S A 99, 7889–7894.
Hagglund, R., and Roizman, B. (2003). Herpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicity. J Virol 77, 13194–13202.
Hagglund, R., and Roizman, B. (2004). Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. J Virol 78, 2169–2178.
Hagglund, R., Van Sant, C., Lopez, P., and Roizman, B. (2002). Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proc Natl Acad Sci U S A 99, 631–636.
Halford, W.P., Kemp, C.D., Isler, J.A., Davido, D.J., and Schaffer, P.A. (2001). ICP0, ICP4, or VP16 expressed from adenovirus vectors induces reactivation of latent herpes simplex virus type 1 in primary cultures of latently infected trigeminal ganglion cells. J Virol 75, 6143–6153.
Halford, W.P., and Schaffer, P.A. (2001). ICP0 is required for efficient reactivation of herpes simplex virus type 1 from neuronal latency. J Virol 75, 3240–3249.
Harris, R.A., and Preston, C.M. (1991). Establishment of latency in vitro by the herpes simplex virus type 1 mutant in1814. J Gen Virol 72, 907–913.
Herrera, F.J., and Triezenberg, S.J. (2004). VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection. J Virol 78, 9689–9696.
Iki, S., Yokota, S., Okabayashi, T., Yokosawa, N., Nagata, K., and Fujii, N. (2005). Serum-dependent expression of promyelocytic leukemia protein suppresses propagation of influenza virus. Virology 343, 106–115.
Ishov, A.M., and Maul, G.G. (1996). The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J Cell Biol 134, 815–826.
Ishov, A.M., Sotnikov, A.G., Negorev, D., Vladimirova, O.V., Neff, N., Kamitani, T., Yeh, E.T., Strauss, J.F. 3rd, and Maul, G.G. (1999). PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J Cell Biol 147, 221–234.
Ishov, A.M., Stenberg, R.M., and Maul, G.G. (1997). Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J Cell Biol 138, 5–16.
Jackson, S.A., and DeLuca, N.A. (2003). Relationship of herpes simplex virus genome configuration to productive and persistent infections. Proc Natl Acad Sci U S A 100, 7871–7876.
Jul-Larsen, A., Visted, T., Karlsen, B.O., Rinaldo, C.H., Bjerkvig, R., Lønning, P.E., and Bøe, S.O. (2004). PML-nuclear bodies accumulate DNA in response to polyomavirus BK and simian virus 40 replication. Exp Cell Res 298, 58–73.
Kamitani, T., Kito, K., Nguyen, H.P., Wada, H., Fukuda-Kamitani, T., and Yeh, E.T. (1998a). Identification of three major sentrinization sites in PML. J Biol Chem 273, 26675–26682.
Kamitani, T., Nguyen, H.P., Kito, K., Fukuda-Kamitani, T., and Yeh, E.T. (1998b). Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J Biol Chem 273, 3117–3120.
Kawaguchi, Y., Bruni, R., and Roizman, B. (1997a). Interaction of herpes simplex virus 1 alpha regulatory protein ICP0 with elongation factor 1delta: ICP0 affects translational machinery. J Virol 71, 1019–1024.
Kawaguchi, Y., Tanaka, M., Yokoymama, A., Matsuda, G., Kato, K., Kagawa, H., Hirai, K., and Roizman, B. (2001). Herpes simplex virus 1 alpha regulatory protein ICP0 functionally interacts with cellular transcription factor BMAL1. Proc Natl Acad Sci U S A 98, 1877–1882.
Kawaguchi, Y., Van Sant, C., and Roizman, B. (1997b). Herpes simplex virus 1 alpha regulatory protein ICP0 interacts with and stabilizes the cell cycle regulator cyclin D3. J Virol 71, 7328–7336.
Klemm, R.D., Goodrich, J.A., Zhou, S., and Tjian, R. (1995). Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. Proc Natl Acad Sci U S A 92, 5788–5792.
Kyratsous, C.A., and Silverstein, S.J. (2009). Components of nuclear domain 10 bodies regulate varicella-zoster virus replication. J Virol 83, 4262–4274.
Lallemand-Breitenbach, V., Zhu, J., Puvion, F., Koken, M., Honoré, N., Doubeikovsky, A., Duprez, E., Pandolfi, P.P., Puvion, E., Freemont, P., et al. (2001). Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J Exp Med 193, 1361–1371.
Lees-Miller, S.P., Long, M.C., Kilvert, M.A., Lam, V., Rice, S.A., and Spencer, C.A. (1996). Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by the herpes simplex virus type 1 transactivator ICP0. J Virol 70, 7471–7477.
Lehman, I.R., and Boehmer, P.E. (1999). Replication of herpes simplex virus DNA. J Biol Chem 274, 28059–28062.
Leib, D.A., Coen, D.M., Bogard, C.L., Hicks, K.A., Yager, D.R., Knipe, D.M., Tyler, K.L., and Schaffer, P.A. (1989). Immediate-early regulatory gene mutants define different stages in the establishment and reactivation of herpes simplex virus latency. J Virol 63, 759–768.
Li, W., Wang, G., Zhang, H., Zhang, D., Zeng, J., Chen, X., Xu, Y., and Li, K. (2009). Differential suppressive effect of promyelocytic leukemia protein on the replication of different subtypes/strains of influenza A virus. Biochem Biophys Res Commun 389, 84–89.
Ling, P.D., Peng, R.S., Nakajima, A., Yu, J.H., Tan, J., Moses, S.M., Yang, W.H., Zhao, B., Kieff, E., Bloch, K.D., et al. (2005). Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100. EMBO J 24, 3565–3575.
Lomonte, P., and Morency, E. (2007). Centromeric protein CENP-B proteasomal degradation induced by the viral protein ICP0. FEBS Lett 581, 658–662.
Lomonte, P., Sullivan, K.F., and Everett, R.D. (2001). Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J Biol Chem 276, 5829–5835.
Lomonte, P., Thomas, J., Texier, P., Caron, C., Khochbin, S., and Epstein, A.L. (2004). Functional interaction between class II histone deacetylases and ICP0 of herpes simplex virus type 1. J Virol 78, 6744–6757.
Lopez, P., Jacob, R.J., and Roizman, B. (2002). Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins. J Virol 76, 9355–9367.
Lukashchuk, V., and Everett, R.D. (2010). Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx. J Virol 84, 4026–4040.
Mahajan, S.S., Little, M.M., Vazquez, R., and Wilson, A.C. (2002). Interaction of HCF-1 with a cellular nuclear export factor. J Biol Chem 277, 44292–44299.
Maul, G.G. (1998). Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20, 660–667.
Maul, G.G., and Everett, R.D. (1994). The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J Gen Virol 75, 1223–1233.
Maul, G.G., Guldner, H.H., and Spivack, J.G. (1993). Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J Gen Virol 74, 2679–2690.
Maul, G.G., Ishov, A.M., and Everett, R.D. (1996). Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology 217, 67–75.
McNally, B.A., Trgovcich, J., Maul, G.G., Liu, Y., and Zheng, P. (2008). A role for cytoplasmic PML in cellular resistance to viral infection. PLoS One 3, e2277.
Memedula, S., and Belmont, A.S. (2003). Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16. Curr Biol 13, 241–246.
Meredith, M., Orr, A., Elliott, M., and Everett, R. (1995). Separation of sequence requirements for HSV-1 Vmw110 multimerisation and interaction with a 135-kDa cellular protein. Virology 209, 174–187.
Mitchell, B.M., Bloom, D.C., Cohrs, R.J., Gilden, D.H., and Kennedy, P.G. (2003). Herpes simplex virus-1 and varicella-zoster virus latency in ganglia. J Neurovirol 9, 194–204.
Mittler, G., Stühler, T., Santolin, L., Uhlmann, T., Kremmer, E., Lottspeich, F., Berti, L., and Meisterernst, M. (2003). A novel docking site on Mediator is critical for activation by VP16 in mammalian cells. EMBO J 22, 6494–6504.
Mossman, K.L., and Smiley, J.R. (2002). Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication. J Virol 76, 1995–1998.
Müller, S., Matunis, M.J., and Dejean, A. (1998). Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J 17, 61–70.
Negorev, D., and Maul, G.G. (2001). Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 20, 7234–7242.
Negorev, D.G., Vladimirova, O.V., Ivanov, A., Rauscher, F. 3rd, and Maul, G.G. (2006). Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression. J Virol 80, 8019–8029.
Negorev, D.G., Vladimirova, O.V., and Maul, G.G. (2009). Differential functions of interferon-upregulated Sp100 isoforms: herpes simplex virus type 1 promoter-based immediate-early gene suppression and PML protection from ICP0-mediated degradation. J Virol 83, 5168–5180.
Pampin, M., Simonin, Y., Blondel, B., Percherancier, Y., and Chelbi-Alix, M.K. (2006). Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense. J Virol 80, 8582–8592.
Parkinson, J., and Everett, R.D. (2000). Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J Virol 74, 10006–10017.
Parkinson, J., Lees-Miller, S.P., and Everett, R.D. (1999). Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J Virol 73, 650–657.
Paterson, T., and Everett, R.D. (1988). Mutational dissection of the HSV-1 immediate-early protein Vmw175 involved in transcriptional transactivation and repression. Virology 166, 186–196.
Preston, C.M. (2000). Repression of viral transcription during herpes simplex virus latency. J Gen Virol 81, 1–19.
Preston, C.M., and Nicholl, M.J. (1997). Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis. J Virol 71, 7807–7813.
Regad, T., and Chelbi-Alix, M.K. (2001). Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20, 7274–7286.
Regad, T., Saib, A., Lallemand-Breitenbach, V., Pandolfi, P.P., de Thé, H., and Chelbi-Alix, M.K. (2001). PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator. EMBO J 20, 3495–3505.
Reichelt, M., Wang, L., Sommer, M., Perrino, J., Nour, A.M., Sen, N., Baiker, A., Zerboni, L., and Arvin, A.M. (2011). Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus. PLoS Pathog 7, e1001266.
Rolley, N., Butcher, S., and Milner, J. (1995). Specific DNA binding by different classes of human p53 mutants. Oncogene 11, 763–770.
Sacks, W.R., and Schaffer, P.A. (1987). Deletion mutants in the gene encoding the herpes simplex virus type 1 immediate-early protein ICP0 exhibit impaired growth in cell culture. J Virol 61, 829–839.
Saffert, R.T., and Kalejta, R.F. (2008). Promyelocytic leukemia-nuclear body proteins: herpesvirus enemies, accomplices, or both? Future Virol 3, 265–277.
Samaniego, L.A., Neiderhiser, L., and DeLuca, N.A. (1998). Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins. J Virol 72, 3307–3320.
Schreiner, S., Wimmer, P., Sirma, H., Everett, R.D., Blanchette, P., Groitl, P., and Dobner, T. (2010). Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells. J Virol 84, 7029–7038.
Seeler, J.S., and Dejean, A. (2001). SUMO: of branched proteins and nuclear bodies. Oncogene 20, 7243–7249.
Shen, T.H., Lin, H.K., Scaglioni, P.P., Yung, T.M., and Pandolfi, P.P. (2006). The mechanisms of PML-nuclear body formation. Mol Cell 24, 331–339.
Shimomura Y. (2008). Herpes simplex virus latency, reactivation, and a new antiviral therapy for herpetic keratitis. Nihon Ganka Gakkai Zasshi 112, 247–264; discussion 265.
Smith, A.E., and Helenius, A. (2004). How viruses enter animal cells. Science 304, 237–242.
Smith, C.A., Bates, P., Rivera-Gonzalez, R., Gu, B., and DeLuca, N.A. (1993). ICP4, the major transcriptional regulatory protein of herpes simplex virus type 1, forms a tripartite complex with TATA-binding protein and TFIIB. J Virol 67, 4676–4687.
Sternsdorf, T., Grötzinger, T., Jensen, K., and Will, H. (1997a). Nuclear dots: actors on many stages. Immunobiology 198, 307–331.
Sternsdorf, T., Jensen, K., Reich, B., and Will, H. (1999). The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J Biol Chem 274, 12555–12566.
Sternsdorf, T., Jensen, K., and Will, H. (1997b). Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J Cell Biol 139, 1621–1634.
Stow, N.D., and Stow, E.C. (1986). Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. J Gen Virol 67, 2571–2585.
Tavalai, N., Papior, P., Rechter, S., Leis, M., and Stamminger, T. (2006). Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J Virol 80, 8006–8018.
Tavalai, N., Papior, P., Rechter, S., and Stamminger, T. (2008). Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. J Virol 82, 126–137.
Tavalai, N., and Stamminger, T. (2008). New insights into the role of the subnuclear structure ND10 for viral infection. Biochim Biophys Acta 1783, 2207–2221.
Van Sant, C., Hagglund, R., Lopez, P., and Roizman, B. (2001). The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity. Proc Natl Acad Sci U S A 98, 8815–8820.
von Einem, J., Schumacher, D., O’Callaghan, D.J., and Osterrieder, N. (2006). The alpha-TIF (VP16) homologue (ETIF) of equine herpesvirus 1 is essential for secondary envelopment and virus egress. J Virol 80, 2609–2620.
Wagner, E.K., and Bloom, D.C. (1997). Experimental investigation of herpes simplex virus latency. Clin Microbiol Rev 10, 419–443.
Watson, R.J., and Clements, J.B. (1980). A herpes simplex virus type 1 function continuously required for early and late virus RNA synthesis. Nature 285, 329–330.
Wiesmeijer, K., Molenaar, C., Bekeer, I.M., Tanke, H.J., and Dirks, R.W. (2002). Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not. J Struct Biol 140, 180–188.
Wysocka, J., and Herr, W. (2003). The herpes simplex virus VP16-induced complex: the makings of a regulatory switch. Trends Biochem Sci 28, 294–304.
Xiao, H., Pearson, A., Coulombe, B., Truant, R., Zhang, S., Regier, J.L., Triezenberg, S.J., Reinberg, D., Flores, O., Ingles, C.J., et al. (1994). Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. Mol Cell Biol 14, 7013–7024.
Yao, F., and Schaffer, P.A. (1995). An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1. J Virol 69, 6249–6258.
Zhong, S., Müller, S., Ronchetti, S., Freemont, P.S., Dejean, A., and Pandolfi, P.P. (2000). Role of SUMO-1-modified PML in nuclear body formation. Blood 95, 2748–2752.
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Wang, S., Long, J. & Zheng, Cf. The potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1. Protein Cell 3, 372–382 (2012). https://doi.org/10.1007/s13238-012-2021-x
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DOI: https://doi.org/10.1007/s13238-012-2021-x