{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:18:09Z","timestamp":1791267489688,"version":"4.1.0"},"reference-count":55,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2011,6,1]],"date-time":"2011-06-01T00:00:00Z","timestamp":1306886400000},"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":[[2011,6]]},"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            resists killing by antimicrobial peptides encountered during human infection, including cathelicidin LL-37, \u03b1-defensins, and \u03b2-defensins. In this study, we examined the role of the proton motive force-dependent multiple transferable resistance (MTR) transporter in antimicrobial peptide resistance in\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            . We found a proton motive force-dependent effect on\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            's resistance to LL-37 and \u03b2-defensin HBD-3, but not \u03b1-defensin HNP-2. Deletion of the membrane fusion protein MtrC rendered\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            more sensitive to LL-37 and human \u03b2-defensins but had relatively little effect on \u03b1-defensin resistance. The\n            <jats:italic>mtrC<\/jats:italic>\n            mutant 35000HP\n            <jats:italic>mtrC<\/jats:italic>\n            exhibited phenotypic changes in outer membrane protein profiles, colony morphology, and serum sensitivity, which were restored to wild type by\n            <jats:italic>trans<\/jats:italic>\n            -complementation with\n            <jats:italic>mtrC<\/jats:italic>\n            . Similar phenotypes were reported in a\n            <jats:italic>cpxA<\/jats:italic>\n            mutant; activation of the two-component CpxRA regulator was confirmed by showing transcriptional effects on CpxRA-regulated genes in 35000HP\n            <jats:italic>mtrC<\/jats:italic>\n            . A\n            <jats:italic>cpxR<\/jats:italic>\n            mutant had wild-type levels of antimicrobial peptide resistance; a\n            <jats:italic>cpxA<\/jats:italic>\n            mutation had little effect on defensin resistance but led to increased sensitivity to LL-37. 35000HP\n            <jats:italic>mtrC<\/jats:italic>\n            was more sensitive than the\n            <jats:italic>cpxA<\/jats:italic>\n            mutant to LL-37, indicating that MTR contributed to LL-37 resistance independent of the CpxRA regulon. The CpxRA regulon did not affect proton motive force-dependent antimicrobial peptide resistance; however, 35000HP\n            <jats:italic>mtrC<\/jats:italic>\n            had lost proton motive force-dependent peptide resistance, suggesting that the MTR transporter promotes proton motive force-dependent resistance to LL-37 and human \u03b2-defensins. This is the first report of a \u03b2-defensin resistance mechanism in\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            and shows that LL-37 resistance in\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            is multifactorial.\n          <\/jats:p>","DOI":"10.1128\/iai.01316-10","type":"journal-article","created":{"date-parts":[[2011,3,29]],"date-time":"2011-03-29T02:06:34Z","timestamp":1301364394000},"page":"2324-2334","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":37,"title":["Deletion of\n            <i>mtrC<\/i>\n            in Haemophilus ducreyi Increases Sensitivity to Human Antimicrobial Peptides and Activates the CpxRA Regulon"],"prefix":"10.1128","volume":"79","author":[{"given":"Sherri D.","family":"Rinker","sequence":"first","affiliation":[{"name":"Departments of Microbiology and Immunology, Indiana University School of Medicine, 635 Barnhill Drive, Room MS 420, Indianapolis, Indiana 46202-5124"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael P.","family":"Trombley","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Immunology, Indiana University School of Medicine, 635 Barnhill Drive, Room MS 420, Indianapolis, Indiana 46202-5124"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoping","family":"Gu","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Immunology, Indiana University School of Medicine, 635 Barnhill Drive, Room MS 420, Indianapolis, Indiana 46202-5124"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kate R.","family":"Fortney","sequence":"additional","affiliation":[{"name":"Medicine, Indiana University School of Medicine, 635 Barnhill Drive, Room MS 420, Indianapolis, Indiana 46202-5124"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margaret E.","family":"Bauer","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Immunology, Indiana University School of Medicine, 635 Barnhill Drive, Room MS 420, Indianapolis, Indiana 46202-5124"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.6.3431-3439.2005"},{"key":"e_1_3_2_3_2","first-page":"36","article-title":"Image processing with ImageJ","volume":"11","author":"Abramoff M. 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