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Architecture of replication compartments formed during Epstein-Barr virus lytic replication.
J Virol. 2005 Mar; 79(6):3409-18.JV

Abstract

Epstein-Barr virus (EBV) productive DNA replication occurs at discrete sites, called replication compartments, in nuclei. In this study we performed comprehensive analyses of the architecture of the replication compartments. The BZLF1 oriLyt binding proteins showed a fine, diffuse pattern of distribution throughout the nuclei at immediate-early stages of induction and then became associated with the replicating EBV genome in the replication compartments during lytic infection. The BMRF1 polymerase (Pol) processivity factor showed a homogenous, not dot-like, distribution in the replication compartments, which completely coincided with the newly synthesized viral DNA. Inhibition of viral DNA replication with phosphonoacetic acid, a viral DNA Pol inhibitor, eliminated the DNA-bound form of the BMRF1 protein, although the protein was sufficiently expressed in the cells. These observations together with the findings that almost all abundantly expressed BMRF1 proteins existed in the DNA-bound form suggest that the BMRF1 proteins not only act at viral replication forks as Pol processive factors but also widely distribute on newly replicated EBV genomic DNA. In contrast, the BALF5 Pol catalytic protein, the BALF2 single-stranded-DNA binding protein, and the BBLF2/3 protein, a component of the helicase-primase complex, were colocalized as distinct dots distributed within replication compartments, representing viral replication factories. Whereas cellular replication factories are constructed based on nonchromatin nuclear structures and nuclear matrix, viral replication factories were easily solubilized by DNase I treatment. Thus, compared with cellular DNA replication, EBV lytic DNA replication factories would be simpler so that construction of the replication domain would be more relaxed.

Authors+Show Affiliations

Division of Virology, Aichi Cancer Center Research Institute, 1-1, Kanokoden, Chikusa-ku, Nagoya 464-8681, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15731235

Citation

Daikoku, Tohru, et al. "Architecture of Replication Compartments Formed During Epstein-Barr Virus Lytic Replication." Journal of Virology, vol. 79, no. 6, 2005, pp. 3409-18.
Daikoku T, Kudoh A, Fujita M, et al. Architecture of replication compartments formed during Epstein-Barr virus lytic replication. J Virol. 2005;79(6):3409-18.
Daikoku, T., Kudoh, A., Fujita, M., Sugaya, Y., Isomura, H., Shirata, N., & Tsurumi, T. (2005). Architecture of replication compartments formed during Epstein-Barr virus lytic replication. Journal of Virology, 79(6), 3409-18.
Daikoku T, et al. Architecture of Replication Compartments Formed During Epstein-Barr Virus Lytic Replication. J Virol. 2005;79(6):3409-18. PubMed PMID: 15731235.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Architecture of replication compartments formed during Epstein-Barr virus lytic replication. AU - Daikoku,Tohru, AU - Kudoh,Ayumi, AU - Fujita,Masatoshi, AU - Sugaya,Yutaka, AU - Isomura,Hiroki, AU - Shirata,Noriko, AU - Tsurumi,Tatsuya, PY - 2005/2/26/pubmed PY - 2005/4/6/medline PY - 2005/2/26/entrez SP - 3409 EP - 18 JF - Journal of virology JO - J Virol VL - 79 IS - 6 N2 - Epstein-Barr virus (EBV) productive DNA replication occurs at discrete sites, called replication compartments, in nuclei. In this study we performed comprehensive analyses of the architecture of the replication compartments. The BZLF1 oriLyt binding proteins showed a fine, diffuse pattern of distribution throughout the nuclei at immediate-early stages of induction and then became associated with the replicating EBV genome in the replication compartments during lytic infection. The BMRF1 polymerase (Pol) processivity factor showed a homogenous, not dot-like, distribution in the replication compartments, which completely coincided with the newly synthesized viral DNA. Inhibition of viral DNA replication with phosphonoacetic acid, a viral DNA Pol inhibitor, eliminated the DNA-bound form of the BMRF1 protein, although the protein was sufficiently expressed in the cells. These observations together with the findings that almost all abundantly expressed BMRF1 proteins existed in the DNA-bound form suggest that the BMRF1 proteins not only act at viral replication forks as Pol processive factors but also widely distribute on newly replicated EBV genomic DNA. In contrast, the BALF5 Pol catalytic protein, the BALF2 single-stranded-DNA binding protein, and the BBLF2/3 protein, a component of the helicase-primase complex, were colocalized as distinct dots distributed within replication compartments, representing viral replication factories. Whereas cellular replication factories are constructed based on nonchromatin nuclear structures and nuclear matrix, viral replication factories were easily solubilized by DNase I treatment. Thus, compared with cellular DNA replication, EBV lytic DNA replication factories would be simpler so that construction of the replication domain would be more relaxed. SN - 0022-538X UR - https://www.unboundmedicine.com/medline/citation/15731235/Architecture_of_replication_compartments_formed_during_Epstein_Barr_virus_lytic_replication_ L2 - http://jvi.asm.org/cgi/pmidlookup?view=long&pmid=15731235 DB - PRIME DP - Unbound Medicine ER -