{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T05:04:05Z","timestamp":1791263045284,"version":"4.1.0"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2008,4,1]],"date-time":"2008-04-01T00:00:00Z","timestamp":1207008000000},"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":[[2008,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The ability to bind extracellular matrix proteins is a critical virulence determinant for skin pathogens.\n            <jats:italic>Haemophilus ducreyi<\/jats:italic>\n            , the etiological agent of the genital ulcer disease chancroid, binds extracellular matrix components, including fibronectin (FN). We investigated\n            <jats:italic>H. ducreyi<\/jats:italic>\n            FN binding and report several important findings about this interaction. First, FN binding by\n            <jats:italic>H. ducreyi<\/jats:italic>\n            was greatly increased in bacteria grown on heme and almost completely inhibited by hemoglobin. Second, wild-type strain 35000HP bound significantly more FN than did a\n            <jats:italic>dsrA<\/jats:italic>\n            mutant in two different FN binding assays. Third, the expression of\n            <jats:italic>dsrA<\/jats:italic>\n            in the\n            <jats:italic>dsrA<\/jats:italic>\n            mutant restored FN binding and conferred the ability to bind FN to a non-FN-binding\n            <jats:italic>Haemophilus influenzae<\/jats:italic>\n            strain. Fourth, an anti-DsrA monoclonal antibody partially blocked FN binding by\n            <jats:italic>H. ducreyi<\/jats:italic>\n            . The hemoglobin receptor, the collagen-binding protein, the\n            <jats:italic>H. ducreyi<\/jats:italic>\n            lectin, the fine-tangle pili, and the outer membrane protein OmpA2 were not involved in\n            <jats:italic>H. ducreyi<\/jats:italic>\n            FN binding, since single mutants bound FN as well as the parent strain did. However, the major outer membrane protein may have a minor role in FN binding by\n            <jats:italic>H. ducreyi<\/jats:italic>\n            , since a double\n            <jats:italic>dsrA momp<\/jats:italic>\n            mutant bound less FN than did the single\n            <jats:italic>dsrA<\/jats:italic>\n            mutant. Finally, despite major sequence differences, DsrA proteins from both class I and class II\n            <jats:italic>H. ducreyi<\/jats:italic>\n            strains mediated FN and vitronectin binding. We concluded that DsrA is the major factor involved in FN binding by both classes of\n            <jats:italic>H. ducreyi<\/jats:italic>\n            strains.\n          <\/jats:p>","DOI":"10.1128\/iai.00994-07","type":"journal-article","created":{"date-parts":[[2008,1,23]],"date-time":"2008-01-23T01:44:47Z","timestamp":1201052687000},"page":"1608-1616","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["Outer Membrane Protein DsrA Is the Major Fibronectin-Binding Determinant of\n            <i>Haemophilus ducreyi<\/i>"],"prefix":"10.1128","volume":"76","author":[{"given":"Isabelle","family":"Leduc","sequence":"first","affiliation":[{"name":"Departments of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. 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