{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T09:45:47Z","timestamp":1791107147788,"version":"4.1.0"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"11","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1989,6]]},"abstract":"<jats:p>Toxic shock syndrome toxin 1 (TSST-1) is a 22-kDa exotoxin produced by strains of Staphylococcus aureus and implicated in the pathogenesis of toxic shock syndrome. In common with other staphylococcal exotoxins, TSST-1 has diverse immunological effects. These include the induction of interleukin 2 receptor expression, interleukin 2 synthesis, proliferation of human T lymphocytes, and stimulation of interleukin 1 synthesis by human monocytes. In the present study, we demonstrate that TSST-1 binds with saturation kinetics and with a dissociation constant of 17-43 nM to a single class of binding sites on human mononuclear cells. There was a strong correlation between the number of TSST-1 binding sites and the expression of major histocompatibility complex class II molecules, and interferon-gamma induced the expression of class II molecules as well as TSST-1 binding sites on human skin-derived fibroblasts. Monoclonal antibodies to HLA-DR, but not to HLA-DP or HLA-DQ, strongly inhibited TSST-1 binding. Affinity chromatography of 125I-labeled cell membranes over TSST-1-agarose resulted in the recovery of two bands of 35 kDa and 31 kDa that comigrated, respectively, with the alpha and beta chains of HLA-DR and that could be immunoprecipitated with anti-HLA-DR monoclonal antibodies. Binding of TSST-1 was demonstrated to HLA-DR and HLA-DQ L-cell transfectants. These results indicate that major histocompatibility complex class II molecules represent the major binding site for TSST-1 on human cells.<\/jats:p>","DOI":"10.1073\/pnas.86.11.4210","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T06:56:42Z","timestamp":1149058602000},"page":"4210-4214","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":86,"title":["Toxic shock syndrome toxin 1 binds to major histocompatibility complex class II molecules."],"prefix":"10.1073","volume":"86","author":[{"given":"P","family":"Scholl","sequence":"first","affiliation":[{"name":"Division of Allergy and Immunology, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Diez","sequence":"additional","affiliation":[{"name":"Division of Allergy and Immunology, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W","family":"Mourad","sequence":"additional","affiliation":[{"name":"Division of Allergy and Immunology, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J","family":"Parsonnet","sequence":"additional","affiliation":[{"name":"Division of Allergy and Immunology, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R S","family":"Geha","sequence":"additional","affiliation":[{"name":"Division of Allergy and Immunology, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T","family":"Chatila","sequence":"additional","affiliation":[{"name":"Division of Allergy and Immunology, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1989,6]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.86.11.4210","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T12:58:52Z","timestamp":1649854732000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.86.11.4210"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,6]]},"references-count":0,"journal-issue":{"issue":"11","published-print":{"date-parts":[[1989,6]]}},"alternative-id":["10.1073\/pnas.86.11.4210"],"URL":"https:\/\/doi.org\/10.1073\/pnas.86.11.4210","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,6]]},"assertion":[{"value":"1989-06-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}