{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:22:05Z","timestamp":1790518925219,"version":"4.1.0"},"reference-count":73,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2018,3,1]],"date-time":"2018-03-01T00:00:00Z","timestamp":1519862400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100000925","name":"Department of Health | National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1092262"],"award-info":[{"award-number":["1092262"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"publisher","award":["FL130100038"],"award-info":[{"award-number":["FL130100038"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2018,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The \u03b2-barrel assembly machinery (BAM) complex is the core machinery for the assembly of \u03b2-barrel membrane proteins, and inhibition of BAM complex activity is lethal to bacteria. Discovery of integral membrane proteins that are key to pathogenesis and yet do not require assistance from the BAM complex raises the question of how these proteins assemble into bacterial outer membranes. Here, we address this question through a structural analysis of the type 2 secretion system (T2SS) secretin from enteropathogenic\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            O127:H6 strain E2348\/69. Long \u03b2-strands assemble into a barrel extending 17 \u212b through and beyond the outer membrane, adding insight to how these extensive \u03b2-strands are assembled into the\n            <jats:named-content content-type=\"genus-species\">E. coli<\/jats:named-content>\n            outer membrane. The substrate docking chamber of this secretin is shown to be sufficient to accommodate the substrate mucinase SteC.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            In order to cause disease, bacterial pathogens inhibit immune responses and induce pathology that will favor their replication and dissemination. In Gram-negative bacteria, these key attributes of pathogenesis depend on structures assembled into or onto the outer membrane. One of these is the T2SS. The\n            <jats:named-content content-type=\"genus-species\">Vibrio<\/jats:named-content>\n            -type T2SS mediates cholera toxin secretion in\n            <jats:named-content content-type=\"genus-species\">Vibrio cholerae<\/jats:named-content>\n            , and in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            O127:H6 strain E2348\/69, the same machinery mediates secretion of the mucinases that enable the pathogen to penetrate intestinal mucus and thereby establish deadly infections.\n          <\/jats:p>","DOI":"10.1128\/jb.00521-17","type":"journal-article","created":{"date-parts":[[2017,10,30]],"date-time":"2017-10-30T15:55:29Z","timestamp":1509378929000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":34,"title":["Structure and Membrane Topography of the Vibrio-Type Secretin Complex from the Type 2 Secretion System of 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