{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,4,25]],"date-time":"2025-04-25T04:12:45Z","timestamp":1745554365009,"version":"3.40.4"},"reference-count":8,"publisher":"S. Karger AG","issue":"5","license":[{"start":{"date-parts":[[2001,1,1]],"date-time":"2001-01-01T00:00:00Z","timestamp":978307200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"},{"start":{"date-parts":[[2001,1,1]],"date-time":"2001-01-01T00:00:00Z","timestamp":978307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Intervirology"],"published-print":{"date-parts":[[2001]]},"abstract":"<i>Objective:<\/i> Epstein-Barr virus (EBV) nuclear antigen-1 (EBNA-1) and the replication origin, <i>oriP<\/i>, are essential for the replication and maintenance of latent EBV DNA in cells, but no enzymatic activity has been associated with EBNA-1 protein alone. In this study, we have searched for host cellular proteins that interact with EBNA-1 protein in various B cell lines latently infected with EBV, including a recently EBV growth-transformed cell line. <i>Methods:<\/i> By using gel shift analysis, we investigated the interactions of an oligonucleotide containing a single EBNA-1 recognition site, derived from the family of repeats (FR) element of <i>oriP<\/i>, with protein from cell extracts. <i>Results:<\/i> The FR oligonucleotide bound a (72-kD) cellular protein in the absence of EBNA-1 and without induction of the previously reported \u2018anti-EBNA-1 proteins\u2019. The FR oligonucleotide formed complexes with additional proteins from EBNA-1-synthesizing cell lines; these complexes were abolished or supershifted by anti-EBNA-1 monoclonal antibodies. SDS-PAGE analyses of <sup>35<\/sup>S-Met-labeled proteins that bound to a biotin- conjugated FR oligonucleotide, fractionated by a glycerol gradient centrifugation and affinity-purified with streptavidin, showed three major bands, a 72-kD protein, the FR binding of which seemed to be independent of EBNA-1, a 64-kD protein in both EBNA-1-transfected and latently EBV-infected cell lines, and a 45-kD protein in EBV-infected cell lines, which was most prominent in a recently EBV growth-transformed cell line. <i>Conclusions:<\/i> The FR element forms complexes with cellular proteins in the absence and presence of EBNA-1. These 72-, 64- and 45-kD cellular proteins might be involved in the function of the <i>oriP<\/i> and EBNA-1 system.<\/jats:p>","DOI":"10.1159\/000050059","type":"journal-article","created":{"date-parts":[[2003,4,15]],"date-time":"2003-04-15T10:10:37Z","timestamp":1050401437000},"page":"283-290","source":"Crossref","is-referenced-by-count":5,"title":["Epstein-Barr Virus Nuclear Antigen-1-Dependent and -Independent <i>oriP<\/i>-Binding Cellular Proteins"],"prefix":"10.1159","volume":"44","author":[{"given":"Shuichi","family":"Kusano","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keiko","family":"Tamada","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hidenobu","family":"Senpuku","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shizuko","family":"Harada","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sayuri","family":"Ito","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kazuo","family":"Yanagi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"127","published-online":{"date-parts":[[2001,10,25]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.51.33009"},{"key":"ref2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/17.21.6394"},{"key":"ref3","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1521-1878(199901)21:1<5::AID-BIES2>3.0.CO;2-6"},{"key":"ref4","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.63.1.745"},{"key":"ref5","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.74.10.4512-4522.2000"},{"key":"ref6","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.7.3999"},{"key":"ref7","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.22.12041"},{"key":"ref8","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1999.9854"}],"container-title":["Intervirology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.karger.com\/Article\/Pdf\/50059","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.karger.com\/Article\/Pdf\/50059","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,4,24]],"date-time":"2025-04-24T04:19:37Z","timestamp":1745468377000},"score":1,"resource":{"primary":{"URL":"https:\/\/karger.com\/article\/doi\/10.1159\/000050059"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001]]},"references-count":8,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2001,10,1]]}},"URL":"https:\/\/doi.org\/10.1159\/000050059","archive":["Portico"],"relation":{},"ISSN":["0300-5526","1423-0100"],"issn-type":[{"type":"print","value":"0300-5526"},{"type":"electronic","value":"1423-0100"}],"subject":[],"published":{"date-parts":[[2001]]}}}