{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,27]],"date-time":"2023-10-27T08:12:25Z","timestamp":1698394345633},"reference-count":30,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":4535,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1996,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Toxic shock syndrome toxin\u20101 (TSST\u20101) is one of a family of staphylococcal exotoxins recognized as microbial superantigens. The toxin plays a dominant role in the genesis of toxic shock in humans through a massive activation of the immune system. This potentially lethal illness occurs as a result of the interaction of TSST\u20101 with a significant proportion of the T\u2010cell repertoire. TSST\u20101, like other superantigens, can bind directly to class II major histocompatibility (MHC class II) molecules prior to its interaction with entire families of <jats:italic>V\u03b2<\/jats:italic> chains of the T\u2010cell receptor (TCR). The three\u2010dimensional structure of a mutant (His\u2010135\u2010Ala) TSST\u20101 was compared with the structure of the native (wild\u2010type) TSST\u20101 at 2.5 \u00c5 resolution. The replacement of His 135 of TSST\u20101 with an Ala residue results in the loss of T\u2010cell mitogenicity and toxicity in experimental animals. This residue, postulated to be directly involved in the toxin\u2010TCR interactions, is located on the major helix \u03b12, which forms the backbone of the molecule and is exposed to the solvent. In the molecular structure of the mutant toxin, the helix \u03b12 remains unaltered, but the His to Ala modification causes perturbations on the neighboring helix \u03b11 by disrupting helix\u2010helix interactions. Thus, the effects on TCR binding of the His 135 residue could actually be mediated, wholly or in part, by the \u03b11 helix.<\/jats:p>","DOI":"10.1002\/pro.5560050826","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T03:48:07Z","timestamp":1234237687000},"page":"1737-1741","source":"Crossref","is-referenced-by-count":8,"title":["Crystal structure of a biologically inactive mutant of toxic shock syndrome toxin\u20101 at 2.5 A resolution"],"prefix":"10.1002","volume":"5","author":[{"given":"Anastassios C.","family":"Papageorgiou","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Conrad P.","family":"Quinn","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Beer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rossalyn D.","family":"Brehm","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Howard S.","family":"Tranter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter F.","family":"Bonventre","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K.Ravi","family":"Acharya","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"3901","DOI":"10.1002\/j.1460-2075.1985.tb04164.x","article-title":"Analysis of signals for secretion in the staphylococcal protein A gene","volume":"4","author":"Abrahamsen L","year":"1985","journal-title":"EMBO J"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/367094a0"},{"key":"e_1_2_1_4_1","first-page":"367","volume-title":"Sourcebook of bacterial protein toxins","author":"Alouf JE","year":"1991"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(84)91241-8"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/iai.61.3.793-799.1993"},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1128\/iai.63.2.509-515.1995","article-title":"A mutation of histidine residue 135 of toxic shock syndrome toxin yields an immunogenic protein with minimal toxicity","volume":"63","author":"Bonventre PF","year":"1995","journal-title":"Infect Immun"},{"key":"e_1_2_1_8_1","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1128\/aem.56.4.1067-1072.1990","article-title":"Large scale purification of SEA, B and C2 by dye\u2010ligand affinity chromatography","volume":"56","author":"Brehm RD","year":"1990","journal-title":"Appl Environ Microbiol"},{"key":"e_1_2_1_9_1","first-page":"75","volume-title":"Plasmids \u2014 Molecular biological methods for Bacillus","author":"Bron S.","year":"1990"},{"key":"e_1_2_1_10_1","volume-title":"X\u2010PLOR, version 3.1. 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