{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T05:39:04Z","timestamp":1793338744252,"version":"4.5.0"},"reference-count":70,"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            Inhaled\n            <jats:italic>Yersinia pestis<\/jats:italic>\n            produces a severe primary pneumonia known as pneumonic plague, which is contagious and highly lethal to humans and animals. In this study, we first determined the susceptibility of\n            <jats:italic>Y. pestis<\/jats:italic>\n            KIM6 to antimicrobial molecules of the airways. We found that (i) rat bronchoalveolar lavage fluid (rBALF) effectively killed KIM6 cells growing at 37\u00b0C; (ii) the antibacterial components of rBALF were small peptides (&lt;10 kDa) that included two cationic antimicrobial peptides (CAMPs), the rat cathelicidin rCRAMP, and \u03b2-defensin RBD-1; (iii) the human cathelicidin LL-37 killed KIM6 cells as well as rBALF did; and (iv) the bactericidal property of LL-37 was synergistically amplified by human \u03b2-defensin 1, another constitutively expressed pulmonary CAMP. Second, the effects of three major surface proteins of\n            <jats:italic>Y. pestis<\/jats:italic>\n            , namely, the capsular antigen fraction 1 (F1), the pH 6 antigen (Psa fimbriae), and the outer membrane protease Pla, on the bactericidal effect of the antimicrobial rBALF peptides was determined with corresponding deletion mutants. We showed that (i) a\n            <jats:italic>Y. pestis psa<\/jats:italic>\n            mutant was only slightly more susceptible to rBALF than the parental KIM6 strain, (ii) a\n            <jats:italic>caf<\/jats:italic>\n            (F1 gene) mutant and a\n            <jats:italic>caf psa<\/jats:italic>\n            mutant were resistant to rBALF or LL-37, (iii) a\n            <jats:italic>caf pla<\/jats:italic>\n            mutant was as susceptible to the effect of rBALF or LL-37 as KIM6 was (\n            <jats:italic>caf<\/jats:italic>\n            <jats:sup>+<\/jats:sup>\n            <jats:italic>pla<\/jats:italic>\n            <jats:sup>+<\/jats:sup>\n            ), and (iv) only the single\n            <jats:italic>caf<\/jats:italic>\n            mutant (\n            <jats:italic>pla<\/jats:italic>\n            <jats:sup>+<\/jats:sup>\n            ), but not KIM6 or the\n            <jats:italic>caf pla<\/jats:italic>\n            double mutant, degraded LL-37. The activity of Pla toward LL-37 was confirmed with\n            <jats:italic>pla<\/jats:italic>\n            mutants carrying a single-residue substitution affecting plasminogen cleavage. Taken together, our data indicated that Pla might act as a virulence factor not only by processing plasminogen but also by inactivating CAMPs, particularly when F1 is not expressed.\n          <\/jats:p>","DOI":"10.1128\/iai.01197-07","type":"journal-article","created":{"date-parts":[[2008,1,29]],"date-time":"2008-01-29T01:46:26Z","timestamp":1201571186000},"page":"1456-1464","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":62,"title":["Capsular Antigen Fraction 1 and Pla Modulate the Susceptibility of\n            <i>Yersinia pestis<\/i>\n            to Pulmonary Antimicrobial Peptides Such as Cathelicidin"],"prefix":"10.1128","volume":"76","author":[{"given":"Estela M.","family":"Galva\u0301n","sequence":"first","affiliation":[{"name":"Department of Pathobiology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melissa A. S.","family":"Lasaro","sequence":"additional","affiliation":[{"name":"Department of Pathobiology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dieter M.","family":"Schifferli","sequence":"additional","affiliation":[{"name":"Department of Pathobiology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmcl.2007.09.104"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1164\/ajrccm.160.1.9807041"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.01497-06"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111925200"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2005.05.030"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.94.1.19-26.1967"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(77)90000-2"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M206296200"},{"key":"e_1_3_2_10_2","first-page":"27","volume":"306","year":"2006","unstructured":"Bowdish, D. 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