{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,24]],"date-time":"2025-11-24T07:08:08Z","timestamp":1763968088426},"reference-count":40,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2013,12,1]],"date-time":"2013-12-01T00:00:00Z","timestamp":1385856000000},"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":[[2013,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Haemophilus ducreyi<\/jats:named-content>\n            is the etiologic agent of the sexually transmitted genital ulcer disease chancroid. In both natural and experimental chancroid,\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            colocalizes with fibrin at the base of the ulcer. Fibrin is obtained by cleavage of the serum glycoprotein fibrinogen (Fg) by thrombin to initiate formation of the blood clot. Fg binding proteins are critical virulence factors in medically important Gram-positive bacteria.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            has previously been shown to bind Fg in an agglutination assay, and the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            Fg binding protein FgbA was identified in ligand blotting with denatured proteins. To better characterize the interaction of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            with Fg, we examined Fg binding to intact, viable\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            bacteria and identified a novel Fg binding protein.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            bound unlabeled Fg in a dose-dependent manner, as measured by two different methods. In ligand blotting with total denatured cellular proteins, digoxigenin (DIG)-Fg bound only two\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            proteins, the trimeric autotransporter DsrA and the lectin DltA; however, only the isogenic\n            <jats:italic>dsrA<\/jats:italic>\n            mutant had significantly less cell-associated Fg than parental strains in Fg binding assays with intact bacteria. Furthermore, expression of DsrA, but not DltA or an empty vector, rendered the non-Fg-binding\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. influenzae<\/jats:named-content>\n            strain Rd capable of binding Fg. A 13-amino-acid sequence in the C-terminal section of the passenger domain of DsrA appears to be involved in Fg binding by\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            . Taken together, these data suggest that the trimeric autotransporter DsrA is a major determinant of Fg binding at the surface of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">H. ducreyi<\/jats:named-content>\n            .\n          <\/jats:p>","DOI":"10.1128\/iai.00743-13","type":"journal-article","created":{"date-parts":[[2013,9,17]],"date-time":"2013-09-17T03:04:40Z","timestamp":1379387080000},"page":"4443-4452","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":7,"title":["Trimeric Autotransporter DsrA Is a Major Mediator of Fibrinogen Binding in Haemophilus ducreyi"],"prefix":"10.1128","volume":"81","author":[{"given":"William G.","family":"Fusco","sequence":"first","affiliation":[{"name":"Departments of Medicine, University of North Carolina, Chapel Hill, North Carolina, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher","family":"Elkins","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of North Carolina, Chapel Hill, North Carolina, USA"},{"name":"Microbiology and Immunology, University of North Carolina, Chapel Hill, North Carolina, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isabelle","family":"Leduc","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of North Carolina, Chapel Hill, North Carolina, 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