{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T12:31:31Z","timestamp":1770726691651,"version":"3.49.0"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[1995,2,1]],"date-time":"1995-02-01T00:00:00Z","timestamp":791596800000},"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":["Infect Immun"],"published-print":{"date-parts":[[1995,2]]},"abstract":"<jats:p>We have examined the role of the CD4 molecule in primary T-lymphocyte responses to the staphylococcal enterotoxins SEA, SEB, SEC1, and the toxic shock syndrome toxin TSST-1. Proliferating cells were predominantly CD4+; however, the responses to SEA and TSST-1 were most sensitive to inhibition by the anti-CD4 antibody Leu-3a. T-lymphocyte responses to the bacterial superantigens were inhibited by site-directed mutations of residues in the DR beta membrane-proximal domain (DR beta 2) that are also known to be important for interactions with CD4. SEA and TSST-1 binding to DR was reduced by the DR beta 2 mutations and by competition with soluble recombinant CD4. We propose that bacterial superantigens sequentially, or simultaneously with CD4, stabilize complexes of T-cell antigen receptors and major histocompatibility complex class II molecules. The superantigen qualities of these toxins may be due, in part, to a molecular mimicry of CD4 and other adhesion molecules.<\/jats:p>","DOI":"10.1128\/iai.63.2.423-429.1995","type":"journal-article","created":{"date-parts":[[2020,1,6]],"date-time":"2020-01-06T18:45:00Z","timestamp":1578336300000},"page":"423-429","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":23,"title":["Staphylococcal enterotoxin A and toxic shock syndrome toxin compete with CD4 for human major histocompatibility complex class II binding"],"prefix":"10.1128","volume":"63","author":[{"given":"S","family":"Bavari","sequence":"first","affiliation":[{"name":"Department of Immunology and Molecular Biology, U.S. Army Medical Research Institute of Infectious Diseases, Frederick, Maryland 21702-5011."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R G","family":"Ulrich","sequence":"additional","affiliation":[{"name":"Department of Immunology and Molecular Biology, U.S. Army Medical Research Institute of Infectious Diseases, Frederick, Maryland 21702-5011."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","container-title":["Infection and Immunity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/iai.63.2.423-429.1995","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/iai.63.2.423-429.1995","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,5]],"date-time":"2022-03-05T08:15:31Z","timestamp":1646468131000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/iai.63.2.423-429.1995"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,2]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1995,2]]}},"alternative-id":["10.1128\/iai.63.2.423-429.1995"],"URL":"https:\/\/doi.org\/10.1128\/iai.63.2.423-429.1995","relation":{},"ISSN":["0019-9567","1098-5522"],"issn-type":[{"value":"0019-9567","type":"print"},{"value":"1098-5522","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,2]]},"assertion":[{"value":"1995-02-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}