{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:18:08Z","timestamp":1791267488030,"version":"4.1.0"},"reference-count":55,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2010,3,1]],"date-time":"2010-03-01T00:00:00Z","timestamp":1267401600000},"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":[[2010,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Haemophilus ducreyi<\/jats:italic>\n                    is an extracellular pathogen of human epithelial surfaces that resists human antimicrobial peptides (APs). The organism's genome contains homologs of genes\n                    <jats:underline>s<\/jats:underline>\n                    ensitive to\n                    <jats:underline>a<\/jats:underline>\n                    ntimicrobial\n                    <jats:underline>p<\/jats:underline>\n                    eptides (\n                    <jats:italic>sap<\/jats:italic>\n                    operon) in nontypeable\n                    <jats:italic>Haemophilus influenzae<\/jats:italic>\n                    . In this study, we characterized the\n                    <jats:italic>sap<\/jats:italic>\n                    -containing loci of\n                    <jats:italic>H. ducreyi<\/jats:italic>\n                    35000HP and demonstrated that\n                    <jats:italic>sapA<\/jats:italic>\n                    is expressed in broth cultures and\n                    <jats:italic>H. ducreyi<\/jats:italic>\n                    -infected tissue;\n                    <jats:italic>sapA<\/jats:italic>\n                    is also conserved among both class I and class II\n                    <jats:italic>H. ducreyi<\/jats:italic>\n                    strains. We constructed a nonpolar\n                    <jats:italic>sapA<\/jats:italic>\n                    mutant of\n                    <jats:italic>H. ducreyi<\/jats:italic>\n                    35000HP, designated 35000HP\n                    <jats:italic>sapA<\/jats:italic>\n                    , and compared the percent survival of wild-type 35000HP and 35000HP\n                    <jats:italic>sapA<\/jats:italic>\n                    exposed to several human APs, including \u03b1-defensins, \u03b2-defensins, and the cathelicidin LL-37. Unlike an\n                    <jats:italic>H. influenzae sapA<\/jats:italic>\n                    mutant, strain 35000HP\n                    <jats:italic>sapA<\/jats:italic>\n                    was not more susceptible to defensins than strain 35000HP was. However, we observed a significant decrease in the survival of strain 35000HP\n                    <jats:italic>sapA<\/jats:italic>\n                    after exposure to LL-37, which was complemented by introducing\n                    <jats:italic>sapA<\/jats:italic>\n                    in\n                    <jats:italic>trans<\/jats:italic>\n                    . Thus, the Sap transporter plays a role in resistance of\n                    <jats:italic>H. ducreyi<\/jats:italic>\n                    to LL-37. We next compared mutant strain 35000HP\n                    <jats:italic>sapA<\/jats:italic>\n                    with strain 35000HP for their ability to cause disease in human volunteers. Although both strains caused papules to form at similar rates, the pustule formation rate at sites inoculated with 35000HP\n                    <jats:italic>sapA<\/jats:italic>\n                    was significantly lower than that of sites inoculated with 35000HP (33.3% versus 66.7%;\n                    <jats:italic>P<\/jats:italic>\n                    = 0.007). Together, these data establish that SapA acts as a virulence factor and as one mechanism for\n                    <jats:italic>H. ducreyi<\/jats:italic>\n                    to resist killing by antimicrobial peptides. To our knowledge, this is the first demonstration that an antimicrobial peptide resistance mechanism contributes to bacterial virulence in humans.\n                  <\/jats:p>","DOI":"10.1128\/iai.01014-09","type":"journal-article","created":{"date-parts":[[2010,1,19]],"date-time":"2010-01-19T23:52:47Z","timestamp":1263945167000},"page":"1176-1184","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":41,"title":["<i>Haemophilus ducreyi<\/i>\n                    SapA Contributes to Cathelicidin Resistance and Virulence in Humans"],"prefix":"10.1128","volume":"78","author":[{"given":"Kristy L. 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