{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T02:17:12Z","timestamp":1789438632188,"version":"build-2803163510"},"reference-count":43,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2015,1,2]],"date-time":"2015-01-02T00:00:00Z","timestamp":1420156800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology of Japan","doi-asserted-by":"publisher","award":["23657087"],"award-info":[{"award-number":["23657087"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology of Japan","doi-asserted-by":"publisher","award":["24370073"],"award-info":[{"award-number":["24370073"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,1,2]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Autoantibodies, including anti-ribosomal P proteins (anti-P), are thought to be produced by an antigen-driven immune response in systemic lupus erythematosus (SLE). To test this hypothesis, we reconstituted the ribosomal antigenic complex in vitro using human P0, phosphorylated P1 and P2 and a 28S rRNA fragment covering the P0 binding site, and immunized Murphy Roths large (MRL)\/lrp lupus mice with this complex without any added adjuvant to generate anti-P antibodies. Using hybridoma technology, we subsequently obtained 34 clones, each producing an anti-P monoclonal antibody (mAb) that recognized the conserved C-terminal tail sequence common to all three P proteins. We also obtained two P0-specific monoclonal antibodies, but no antibody specific to P1, P2 or rRNA fragment. Two types of mAbs were found among these anti-P antibodies: one type (e.g. 9D5) reacted more strongly with the phosphorylated P1 and P2 than that with their non-phosphorylated forms, whereas the other type (e.g. 4H11) reacted equally with both phosphorylated and non-phosphorylated forms of P1\/P2. Both 9D5 and 4H11 inhibited the ribosome\/eukaryotic elongation factor-2 (eEF-2)-coupled guanosine triphosphate (GTP)ase activity. However, preincubation with a synthetic peptide corresponding to the C-terminal sequence common to all three P proteins, but not the peptide that lacked the last three C-terminal amino acids, mostly prevented the mAb-induced inhibition of GTPase activity. Thus, at least two types of anti-P were produced preferentially following the immunization of MRL mice with the reconstituted antigenic complex. Presence of multiple copies of the C-termini, particularly that of the last three C-terminal amino acid residues, in the antigenic complex appears to contribute to the immunogenic stimulus.<\/jats:p>","DOI":"10.1111\/cei.12460","type":"journal-article","created":{"date-parts":[[2014,9,25]],"date-time":"2014-09-25T06:52:21Z","timestamp":1411627941000},"page":"236-244","source":"Crossref","is-referenced-by-count":8,"title":["Characterization of anti-P monoclonal antibodies directed against the ribosomal protein\u2013RNA complex antigen and produced using Murphy Roths large autoimmune-prone mice"],"prefix":"10.1093","volume":"179","author":[{"given":"H","family":"Sato","sequence":"first","affiliation":[{"name":"Division of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Onozuka","sequence":"additional","affiliation":[{"name":"Department of Biology, Faculty of Science, Niigata University, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Hagiya","sequence":"additional","affiliation":[{"name":"Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Ueda, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S","family":"Hoshino","sequence":"additional","affiliation":[{"name":"Department of Biology, Faculty of Science, Niigata University, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"I","family":"Narita","sequence":"additional","affiliation":[{"name":"Division of Clinical Nephrology and Rheumatology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T","family":"Uchiumi","sequence":"additional","affiliation":[{"name":"Department of Biology, Faculty of Science, Niigata University, Niigata, 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