期刊
FEBS JOURNAL
卷 287, 期 1, 页码 205-217出版社
WILEY
DOI: 10.1111/febs.15027
关键词
adenovirus; chromatin; NPM1; nucleolus; ViPR body
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [26440021, 17K07300, 19H04838]
- Equipe FRM [DEQ20180339229]
- Grants-in-Aid for Scientific Research [19H04838, 17K07300, 26440021] Funding Source: KAKEN
The adenovirus (Ad) genome is believed to be packaged into the virion by forming a chromatin-like structure. The replicated viral genome is likely to be condensed through binding with viral core proteins before encapsidation. Replicated viral genomes accumulate in the central region of the nucleus, which we termed virus-induced postreplication (ViPR) body. However, the molecular mechanism by which the nuclear structure is reorganized and its functional significance in virus production are currently not understood. In this study, we found that viral packaging protein IVa2, but not capsid proteins, accumulated in the ViPR body. In addition, nucleolar chromatin regulatory proteins, nucleophosmin 1 (NPM1), upstream binding factor, and nucleolin accumulated in the ViPR body in late-stage Ad infection. NPM1 depletion increased the nuclease-resistant viral genome and delayed the ViPR body formation. These results suggested that structural changes in the infected cell nucleus depend on the formation of viral chromatin by host chromatin regulatory proteins. Because NPM1 depletion decreases production of the infectious virion, we propose that host factor-mediated viral chromatin remodeling and concomitant ViPR body formation are prerequisites for efficient encapsidation of Ad chromatin.
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