{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T23:23:34Z","timestamp":1791069814443,"version":"4.1.0"},"reference-count":43,"publisher":"American Society for Microbiology","issue":"21","license":[{"start":{"date-parts":[[2010,11,1]],"date-time":"2010-11-01T00:00:00Z","timestamp":1288569600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2010,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Coxsackievirus B3 (CVB3) is a small RNA virus associated with diseases such as myocarditis, meningitis, and pancreatitis. We have previously demonstrated that proteasome inhibition reduces CVB3 replication and attenuates virus-induced myocarditis. However, the underlying mechanisms by which the ubiquitin\/proteasome system regulates CVB replication remain unclear. In this study, we investigated the role of REG\u03b3, a member of the 11S proteasome activator, in CVB3 replication. We showed that overexpression of REG\u03b3 promoted CVB3 replication but that knockdown of REG\u03b3 led to reduced CVB3 replication. We further demonstrated that REG\u03b3-mediated p53 proteolysis contributes, as least in part, to the proviral function of REG\u03b3. Although total protein levels of REG\u03b3 remained unaltered after CVB3 infection, virus infection induced a redistribution of REG\u03b3 from the nucleus to the cytoplasm, rendering an opportunity for a direct interaction of REG\u03b3 with viral proteins and\/or host proteins (e.g., p53), which controls viral growth and thereby enhances viral infectivity. Further analyses suggested a potential modification of REG\u03b3 by SUMO following CVB3 infection, which was verified by both\n            <jats:italic>in vitro<\/jats:italic>\n            and\n            <jats:italic>in vivo<\/jats:italic>\n            sumoylation assays. Sumoylation of REG\u03b3 may play a role in its nuclear export during CVB3 infection. Taken together, our results present the first evidence that the host REG\u03b3 pathway is utilized and modified during CVB3 infection to promote efficient viral replication.\n          <\/jats:p>","DOI":"10.1128\/jvi.00008-10","type":"journal-article","created":{"date-parts":[[2010,8,19]],"date-time":"2010-08-19T01:57:29Z","timestamp":1282183049000},"page":"11056-11066","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":37,"title":["Proteasome Activator REG\u03b3 Enhances Coxsackieviral Infection by Facilitating p53 Degradation"],"prefix":"10.1128","volume":"84","author":[{"given":"Guang","family":"Gao","sequence":"first","affiliation":[{"name":"James Hogg Research Center, Providence Heart and Lung Institute, St. Paul's Hospital, and Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC, 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