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Epstein-Barr virus genome packaging factors accumulate in BMRF1-cores within viral replication compartments


Autoři: Atsuko Sugimoto aff001;  Yoriko Yamashita aff004;  Teru Kanda aff001;  Takayuki Murata aff001;  Tatsuya Tsurumi aff001
Působiště autorů: Division of Virology, Aichi Cancer Center Research Institute, Chikusa-ku, Nagoya, Japan aff001;  Department of Virology, Nagoya University Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya, Japan aff002;  Department of Virology and Parasitology, Fujita Health University, School of Medicine, Toyoake, Japan aff003;  Department of Experimental Pathology and Tumor Biology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Japan aff004;  Division of Microbiology, Faculty of Medicine, Tohoku Medical and Pharmaceutical University, Sendai, Japan aff005
Vyšlo v časopise: PLoS ONE 14(9)
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pone.0222519

Souhrn

Productive replication of Epstein-Barr virus (EBV) during the lytic cycle occurs in discrete sites within nuclei, termed replication compartments. We previously proposed that replication compartments consist of two subnuclear domains: “ongoing replication foci” and “BMRF1-cores”. Viral genome replication takes place in ongoing replication foci, which are enriched with viral replication proteins, such as BALF5 and BALF2. Amplified DNA and BMRF1 protein accumulate in BMRF1-cores, which are surrounded by ongoing replication foci. We here determined the locations of procapsid and genome-packaging proteins of EBV via three-dimensional (3D) surface reconstruction and correlative fluorescence microscopy-electron microscopy (FM-EM). The results revealed that viral factors required for DNA packaging, such as BGLF1, BVRF1, and BFLF1 proteins, are located in the innermost subdomains of the BMRF1-cores. In contrast, capsid structural proteins, such as BBRF1, BORF1, BDLF1, and BVRF2, were found both outside and inside the BMRF1-cores. Based on these observations, we propose a model in which viral procapsids are assembled outside the BMRF1-cores and subsequently migrate therein, where viral DNA encapsidation occurs. To our knowledge, this is the first report describing capsid assembly sites in relation to EBV replication compartments.


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