Page 370 - Avian Virology: Current Research and Future Trends

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for cytolytic infection of B cells and maintenance of the transformed Knight, J.S., Sharma, N., and Robertson, E.S. (2005). Epstein-Barr virus
state but not for cytolytic infection of the feather follicle epithelium and latent antigen 3C can mediate the degradation of the retinoblastoma
horizontal spread of MDV. J. Virol. 79, 4545-4549. protein through an SCF cellular ubiquitin ligase. Proc. Natl. Acad. Sci.
Goldstein, D.J., and Weller, S.K. (1988). Herpes simplex virus type 1-induced U.S.A. 102, 18562–18566.
ribonucleotide reductase activity is dispensable for virus growth and Kumar, S., Kunec, D., Buza, J.J., Chiang, H.I., Zhou, H., Subramaniam, S.,
DNA synthesis: isolation and characterization of an ICP6 lacZ insertion Pendarvis, K., Cheng, H.H., and Burgess, S.C. (2012). Nuclear Factor
mutant. J. Virol. 62, 196–205. kappa B is central to Marek’s disease herpesvirus induced neoplastic
Heckert, R.A., Riva, J., Cook, S., McMillen, J., and Schwartz, R.D. (1996). transformation of CD30 expressing lymphocytes in-vivo. BMC Syst.
Onset of protective immunity in chicks after vaccination with a Biol. 6, 123. https://doi.org/10.1186/1752-0509-6-123.
recombinant herpesvirus of turkeys vaccine expressing Newcastle Kut, E., and Rasschaert, D. (2004). Assembly of Marek’s disease virus
disease virus fusion and hemagglutinin-neuraminidase antigens. Avian (MDV) capsids using recombinant baculoviruses expressing MDV
Dis. 40, 770–777. capsid proteins. J. Gen. Virol. 85, 769–774.
Heming, J.D., Conway, J.F., and Homa, F.L. (2017). Herpesvirus capsid Lee, L.F., Wu, P., Sui, D., Ren, D., Kamil, J., Kung, H.J., and Witter, R.L.
assembly and DNA packaging. Adv. Anat. Embryol. Cell Biol. 223, (2000). The complete unique long sequence and the overall genomic
119–142. https://doi.org/10.1007/978-3-319-53168-7_6. organization of the GA strain of Marek’s disease virus. Proc. Natl. Acad.
Hicks, J.A., and Liu, H.C. (2013). Current state of Marek’s disease virus Sci. U.S.A. 97, 6091–6096.
microRNA research. Avian Dis. 57, 332–339. Lee, L.F., Lupiani, B., Silva, R.F., Kung, H.J., and Reddy, S.M. (2008).
Hicks, J.A., Trakooljul, N., and Liu, H.C. (2018). Alterations in cellular Recombinant Marek’s disease virus (MDV) lacking the Meq oncogene
and viral microRNA and cellular gene expression in Marek’s disease confers protection against challenge with a very virulent plus strain of
virus-transformed T-cell lines treated with sodium butyrate. Poult. Sci. MDV. Vaccine 26, 1887–1892.
98, 642–652. Lee, L.F., Kreager, K.S., Arango, J., Paraguassu, A., Beckman, B., Zhang, H.,
Hildebrandt, E., Dunn, J.R., and Cheng, H.H. (2015). Characterizing in vivo Fadly, A., Lupiani, B., and Reddy, S.M. (2010). Comparative evaluation
stability and potential interactions of a UL5 helicase-primase mutation of vaccine efficacy of recombinant Marek’s disease virus vaccine lacking
previously shown to reduce virulence and in vivo replication of Marek’s Meq oncogene in commercial chickens. Vaccine 28, 1294–1299.
disease virus. Virus Res. 203, 1–3. Lee, L.F., Heidari, M., Zhang, H., Lupiani, B., Reddy, S.M., and Fadly, A.
Honess, R.W. (1984). Herpes simplex and ‘the herpes complex’: diverse (2012). Cell culture attenuation eliminates rMd5DeltaMeq-induced
observations and a unifying hypothesis. The eighth Fleming lecture. J. Gen. bursal and thymic atrophy and renders the mutant virus as an effective
Virol. 65, 2077–2107. https://doi.org/10.1099/0022-1317-65-12-2077. and safe vaccine against Marek’s disease. Vaccine 30, 5151–5158.
Isfort, R., Jones, D., Kost, R., Witter, R., and Kung, H.J. (1992). Retrovirus Lee, L.F., Heidari, M., Sun, A., Zhang, H., Lupiani, B., and Reddy, S.
insertion into herpesvirus in vitro and in vivo. Proc. Natl. Acad. Sci. (2013). Identification and in vitro characterization of a Marek’s disease
U.S.A. 89, 991–995. virus-encoded Ribonucleotide reductase. Avian Dis. 57, 178–187.
Iwai, K., Mori, N., Oie, M., Yamamoto, N., and Fujii, M. (2001). Human Levy, A.M., Izumiya, Y., Brunovskis, P., Xia, L., Parcells, M.S., Reddy,
T-cell leukemia virus type 1 tax protein activates transcription through S.M., Lee, L., Chen, H.W., and Kung, H.J. (2003). Characterization of
AP-1 site by inducing DNA binding activity in T-cells. Virology 279, the chromosomal binding sites and dimerization partners of the viral
38–46. https://doi.org/10.1006/viro.2000.0669. oncoprotein Meq in Marek’s disease virus-transformed T-cells. J. Virol.
Izumiya, Y., Jang, H.K., Ono, M., and Mikami, T. (2001). A complete 77, 12841–12851.
genomic DNA sequence of Marek’s disease virus type 2, strain HPRS24. Levy, A.M., Gilad, O., Xia, L., Izumiya, Y., Choi, J., Tsalenko, A., Yakhini,
Curr. Top. Microbiol. Immunol. 255, 191–221. Z., Witter, R., Lee, L., Cardona, C.J., et al. (2005). Marek’s disease virus
Jarosinski, K.W., and Vautherot, J.F. (2015). Differential expression of Marek’s Meq transforms chicken cells via the v-Jun transcriptional cascade: a
disease virus (MDV) late proteins during in vitro and in situ replication: converging transforming pathway for avian oncoviruses. Proc. Natl.
role for pUL47 in regulation of the MDV UL46-UL49 gene locus. Acad. Sci. U.S.A. 102, 14831–14836.
Virology 484, 213–226. https://doi.org/10.1016/j.virol.2015.06.012. Levy-Barda, A., Lerenthal, Y., Davis, A.J., Chung, Y.M., Essers, J., Shao, Z.,
Jones, D., Lee, L., Liu, J.L., Kung, H.J., and Tillotson, J.K. (1992). Marek van Vliet, N., Chen, D.J., Hu, M.C., Kanaar, R., et al. (2011). Involvement
disease virus encodes a basic-leucine zipper gene resembling the fos/jun of the nuclear proteasome activator PA28γ in the cellular response to
oncogenes that is highly expressed in lymphoblastoid tumors. Proc. Natl. DNA double-strand breaks. Cell Cycle 10, 4300–4310. https://doi.
Acad. Sci. U.S.A. 89, 4042–4046. org/10.4161/cc.10.24.18642.
Kaiser, P., Poh, T.Y., Rothwell, L., Avery, S., Balu, S., Pathania, U.S., Hughes, Liu, H.M., Qin, A.J., Liu, Y.L., Jin, W.J., Ye, J.Q., Chen, H.J., Shao, H.X., and
S., Goodchild, M., Morrell, S., Watson, M., et al. (2005). A genomic Li, Y.X. (2006). [Construction and immunological characterization of
analysis of chicken cytokines and chemokines. J. Interferon Cytokine recombinant Marek’s disease virus expressing IBDV VP2 fusion protein].
Res. 25, 467–484. https://doi.org/10.1089/jir.2005.25.467. Sheng Wu Gong Cheng Xue Bao 22, 391–396.
Kamil, J.P., Tischer, B.K., Trapp, S., Nair, V.K., Osterrieder, N., and Kung, Lupiani, B., Lee, L.F., Cui, X., Gimeno, I., Anderson, A., Morgan, R.W., Silva,
H.J. (2005). vLIP, a viral lipase homologue, is a virulence factor of R.F., Witter, R.L., Kung, H.J., and Reddy, S.M. (2004). Marek’s disease
Marek’s disease virus. J. Virol. 79, 6984–6996. virus-encoded Meq gene is involved in transformation of lymphocytes
Kato, K., Jang, H.K., Izumiya, Y., Cai, J.S., Tsushima, Y., Miyazawa, T., Kai, but is dispensable for replication. Proc. Natl. Acad. Sci. U.S.A. 101,
C., and Mikami, T. (1999). Identification of the Marek’s disease virus 11815–11820. https://doi.org/10.1073/pnas.0404508101.
serotype 2 genes homologous to the glycoprotein B (UL27), ICP18.5 Lupiani, B., Lee, L.F., Kreager, K.S., Witter, R.L., and Reddy, S.M. (2013).
(UL28) and major DNA-binding protein (UL29) genes of herpes Insertion of reticuloendotheliosis virus long terminal repeat into the
simplex virus type 1. J. Vet. Med. Sci. 61, 1161–1165. genome of CVI988 strain of Marek’s disease virus results in enhanced
Kaufer, B.B., Trapp, S., Jarosinski, K.W., and Osterrieder, N. (2010). growth and protection. Avian Dis. 57, 427–431.
Herpesvirus telomerase RNA(vTR)-dependent lymphoma formation Mallette, F.A., Mattiroli, F., Cui, G., Young, L.C., Hendzel, M.J., Mer, G.,
does not require interaction of vTR with telomerase reverse transcriptase Sixma, T.K., and Richard, S. (2012). RNF8- and RNF168-dependent
(TERT). PLOS Pathog. 6, e1001073. degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA
Kawamura, H., King, D.J., and Anderson, D.P. (1969). A herpesvirus isolated damage sites. EMBO J. 31, 1865–1878. https://doi.org/10.1038/
from kidney cell culture of normal turkeys. Avian Dis. 13, 853–863. emboj.2012.47.
Kelly, B.J., Fraefel, C., Cunningham, A.L., and Diefenbach, R.J. (2009). Mao, X., Orchard, G., Lillington, D.M., Russell-Jones, R., Young, B.D.,
Functional roles of the tegument proteins of herpes simplex virus and Whittaker, S.J. (2003). Amplification and overexpression of JUNB
type 1. Virus Res. 145, 173–186. https://doi.org/10.1016/j. is associated with primary cutaneous T-cell lymphomas. Blood 101,
virusres.2009.07.007. 1513–1519. https://doi.org/10.1182/blood-2002-08-2434.
Kheimar, A., Previdelli, R.L., Wight, D.J., and Kaufer, B.B. (2017). Telomeres Marek, J. (1907). Multiple Nervenentzündung (Polyneuritis) bei Hühnern.
and Telomerase: Role in Marek’s Disease Virus Pathogenesis, Integration Dtsch. Tierarztl. Wochenschr. 15, 417–421.
and Tumorigenesis. Viruses 9, E173.