{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T12:53:16Z","timestamp":1761742396589},"reference-count":0,"publisher":"Rockefeller University Press","issue":"1","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1988,1,1]]},"abstract":"<jats:p>Two hybridomas that produce the mAbs 135 and 449 B4 were obtained that inhibited the binding of IgE to the Fc epsilon RL\/CD23 on the EBV-transformed B cell line RPMI 8866. mAb 135 was obtained from a mouse immunized with RPMI 8866 cells, whereas mAb 449B4 was obtained from a mouse immunized with a partially purified preparation of Fc epsilon RL\/CD23 obtained as the eluate of an IgE immunoabsorbent loaded with a soluble extract of RPMI 8866 cells. These two mAbs bound to Fc epsilon RL\/CD23- cell lines and precipitated two polypeptides with 36,000 Mr and 28,000 Mr, which were the HLA-DR alpha and beta chains, respectively. Immunoprecipitation with mAb 135 of NP-40 lysates from dithio-bis(succinimidyl propionate) (DSP) crosslinked 125I-labeled RPMI 8866 or normal B cells incubated with rIL-4 showed three polypeptides with 42,000, 36,000, and 28,000 Mr. The 42,000 Mr polypeptide is identical to the Fc epsilon RL\/CD23 since it could be precipitated by the anti-Fc epsilon RL\/CD23 mAb 25 after resolubilization from the SDS-PAGE gel. Immunoprecipitations of the crosslinked cell extracts carried out with the anti-Fc epsilon RL\/CD23 mAb 25 yielded the same three polypeptides. Furthermore, when RPMI 8866 or rIL-4 preincubated normal B cells were solubilized with a digitonin buffer, which prevents the dissociation of noncovalently linked polypeptide complexes, mAb 135 and mAb 25 precipitated complexes composed of three molecules with 42,000, 36,000, and 28,000 Mr. The well-characterized anti-HLA-DR mAb L243 was unable to block the binding of either IgE or mAb 135 to RPMI 8866 cells, although it could immunoprecipitate the complex (HLA-DR-Fc epsilon RL\/CD23) from crosslinked cell lysates. Since mAb 135 and L243 were able to both bind the RPMI 8866 cells, it demonstrates that they bind to different epitopes of the HLA-DR complex, the mAb 135 epitope of the HLA-DR molecule being close to the IgE binding site of the Fc epsilon RL\/CD23. These data demonstrated that the Fc epsilon RL\/CD23 and HLA-DR antigens are spatially associated on the B cell membrane.<\/jats:p>","DOI":"10.1084\/jem.167.1.57","type":"journal-article","created":{"date-parts":[[2004,6,24]],"date-time":"2004-06-24T07:56:10Z","timestamp":1088063770000},"page":"57-72","update-policy":"http:\/\/dx.doi.org\/10.1084\/jem.crossmarkpolicy","source":"Crossref","is-referenced-by-count":84,"title":["The low-affinity receptor for IgE (CD23) on B lymphocytes is spatially associated with HLA-DR antigens."],"prefix":"10.1084","volume":"167","author":[{"given":"J Y","family":"Bonnefoy","sequence":"first","affiliation":[{"name":"UNICET, Laboratory for Immunological Research, Dardilly, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"O","family":"Guillot","sequence":"additional","affiliation":[{"name":"UNICET, Laboratory for Immunological Research, Dardilly, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H","family":"Spits","sequence":"additional","affiliation":[{"name":"UNICET, Laboratory for Immunological Research, Dardilly, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D","family":"Blanchard","sequence":"additional","affiliation":[{"name":"UNICET, Laboratory for Immunological Research, Dardilly, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K","family":"Ishizaka","sequence":"additional","affiliation":[{"name":"UNICET, Laboratory for Immunological Research, Dardilly, France."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J","family":"Banchereau","sequence":"additional","affiliation":[{"name":"UNICET, Laboratory for Immunological Research, Dardilly, France."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[1988,1,1]]},"container-title":["The Journal of experimental medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jem\/article-pdf\/167\/1\/57\/1668439\/57.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jem\/article-pdf\/167\/1\/57\/1668439\/57.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,25]],"date-time":"2023-07-25T01:17:25Z","timestamp":1690247845000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jem\/article\/167\/1\/57\/23708\/The-low-affinity-receptor-for-IgE-CD23-on-B"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1988,1,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1988,1,1]]}},"URL":"https:\/\/doi.org\/10.1084\/jem.167.1.57","relation":{},"ISSN":["0022-1007","1540-9538"],"issn-type":[{"value":"0022-1007","type":"print"},{"value":"1540-9538","type":"electronic"}],"subject":[],"published":{"date-parts":[[1988,1,1]]}}}