{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T22:22:02Z","timestamp":1792794122538,"version":"4.5.0"},"reference-count":48,"publisher":"Springer Science and Business Media LLC","issue":"1","content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Microbiol"],"published-print":{"date-parts":[[2011,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background<\/jats:title><jats:p>Chronic, infected wounds typically contain multiple genera of bacteria, including<jats:italic>Staphylococcus aureus<\/jats:italic>, many of which are strong biofilm formers. Bacterial biofilms are thought to be a direct impediment to wound healing. New therapies that focus on a biofilm approach may improve the recovery and healing rate for infected wounds. In this study, cathelicidins and related short, synthetic peptides were tested for their anti-microbial effectiveness as well as their ability to inhibit the ability of<jats:italic>S. aureus<\/jats:italic>to form biofilms.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>The helical human cathelicidin LL-37 was tested against<jats:italic>S. aureus<\/jats:italic>, and was found to exhibit effective anti-microbial, anti-attachment as well as anti-biofilm activity at concentrations in the low \u03bcg\/ml range. The effect of peptide chirality and associated protease-resistance was explored through the use of an all-D amino acid peptide, D-LL-37, and in turn compared to scrambled LL-37. Helical cathelicidins have been identified in other animals such as the Chinese cobra,<jats:italic>Naja atra<\/jats:italic>(NA-CATH). We previously identified an 11-residue imperfectly repeated pattern (ATRA motif) within the sequence of NA-CATH. A series of short peptides (ATRA-1, -2, -1A), as well as a synthetic peptide, NA-CATH:ATRA1-ATRA1, were designed to explore the significance of the conserved residues within the ATRA motif for anti-microbial activity. The CD spectrum of NA-CATH and NA-CATH:ATRA1-ATRA1 revealed the structural properties of these peptides and suggested that helicity may factor into their anti-microbial and anti-biofilm activities.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions<\/jats:title><jats:p>The NA-CATH:ATRA1-ATRA1 peptide inhibits the production of biofilm by<jats:italic>S. aureus<\/jats:italic>in the presence of salt, exhibiting anti-biofilm activity at lower peptide concentrations than NA-CATH, LL-37 and D-LL-37; and demonstrates low cytoxicity against host cells but does not affect bacterial attachment. The peptides utilized in this anti-biofilm approach may provide templates for a new group of anti-microbials and potential future topical therapeutics for treating chronic wound infections.<\/jats:p><\/jats:sec>","DOI":"10.1186\/1471-2180-11-114","type":"journal-article","created":{"date-parts":[[2011,5,24]],"date-time":"2011-05-24T06:49:40Z","timestamp":1306219780000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":189,"title":["Natural and synthetic cathelicidin peptides with anti-microbial and anti-biofilm activity against Staphylococcus aureus"],"prefix":"10.1186","volume":"11","author":[{"given":"Scott N","family":"Dean","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barney M","family":"Bishop","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monique L","family":"van Hoek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2011,5,23]]},"reference":[{"issue":"8","key":"1406_CR1","doi-asserted-by":"publisher","first-page":"5241","DOI":"10.1128\/IAI.73.8.5241-5244.2005","volume":"73","author":"BE Menzies","year":"2005","unstructured":"Menzies BE, Kenoyer A: Staphylococcus aureus infection of epidermal keratinocytes promotes expression of innate antimicrobial peptides. Infection and immunity. 2005, 73 (8): 5241-5244. 10.1128\/IAI.73.8.5241-5244.2005.","journal-title":"Infection and immunity"},{"issue":"2","key":"1406_CR2","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1007\/s00430-002-0124-3","volume":"191","author":"JK Knobloch","year":"2002","unstructured":"Knobloch JK, Horstkotte MA, Rohde H, Mack D: Evaluation of different detection methods of biofilm formation in Staphylococcus aureus. Medical microbiology and immunology. 2002, 191 (2): 101-106. 10.1007\/s00430-002-0124-3.","journal-title":"Medical microbiology and immunology"},{"issue":"8","key":"1406_CR3","doi-asserted-by":"publisher","first-page":"520","DOI":"10.1056\/NEJM199808203390806","volume":"339","author":"FD Lowy","year":"1998","unstructured":"Lowy FD: Staphylococcus aureus infections. The New England journal of medicine. 1998, 339 (8): 520-532. 10.1056\/NEJM199808203390806.","journal-title":"The New England journal of medicine"},{"issue":"15","key":"1406_CR4","doi-asserted-by":"publisher","first-page":"1763","DOI":"10.1001\/jama.298.15.1763","volume":"298","author":"RM Klevens","year":"2007","unstructured":"Klevens RM, Morrison MA, Nadle J, Petit S, Gershman K, Ray S, Harrison LH, Lynfield R, Dumyati G, Townes JM, et al: Invasive methicillin-resistant Staphylococcus aureus infections in the United States. Jama. 2007, 298 (15): 1763-1771. 10.1001\/jama.298.15.1763.","journal-title":"Jama"},{"issue":"9","key":"1406_CR5","doi-asserted-by":"crossref","first-page":"2206","DOI":"10.1128\/AAC.42.9.2206","volume":"42","author":"J Turner","year":"1998","unstructured":"Turner J, Cho Y, Dinh NN, Waring AJ, Lehrer RI: Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrobial agents and chemotherapy. 1998, 42 (9): 2206-2214.","journal-title":"Antimicrobial agents and chemotherapy"},{"issue":"1","key":"1406_CR6","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1111\/j.1524-475X.2007.00321.x","volume":"16","author":"GA James","year":"2008","unstructured":"James GA, Swogger E, Wolcott R, Pulcini E, Secor P, Sestrich J, Costerton JW, Stewart PS: Biofilms in chronic wounds. Wound Repair Regen. 2008, 16 (1): 37-44. 10.1111\/j.1524-475X.2007.00321.x.","journal-title":"Wound Repair Regen"},{"issue":"2","key":"1406_CR7","doi-asserted-by":"publisher","first-page":"45","DOI":"10.12968\/jowc.2010.19.2.46966","volume":"19","author":"RD Wolcott","year":"2010","unstructured":"Wolcott RD, Rhoads DD, Bennett ME, Wolcott BM, Gogokhia L, Costerton JW, Dowd SE: Chronic wounds and the medical biofilm paradigm. J Wound Care. 2010, 19 (2): 45-46. 48-50, 52-43","journal-title":"J Wound Care"},{"issue":"6870","key":"1406_CR8","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1038\/415389a","volume":"415","author":"M Zasloff","year":"2002","unstructured":"Zasloff M: Antimicrobial peptides of multicellular organisms. Nature. 2002, 415 (6870): 389-395. 10.1038\/415389a.","journal-title":"Nature"},{"issue":"1","key":"1406_CR9","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1124\/pr.55.1.2","volume":"55","author":"MR Yeaman","year":"2003","unstructured":"Yeaman MR, Yount NY: Mechanisms of antimicrobial peptide action and resistance. Pharmacological reviews. 2003, 55 (1): 27-55. 10.1124\/pr.55.1.2.","journal-title":"Pharmacological reviews"},{"issue":"3","key":"1406_CR10","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1038\/nrmicro1098","volume":"3","author":"KA Brogden","year":"2005","unstructured":"Brogden KA: Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nature reviews. 2005, 3 (3): 238-250. 10.1038\/nrmicro1098.","journal-title":"Nature reviews"},{"key":"1406_CR11","doi-asserted-by":"crossref","unstructured":"Niyonsaba F, Ushio H, Hara M, Yokoi H, Tominaga M, Takamori K, Kajiwara N, Saito H, Nagaoka I, Ogawa H, et al: Antimicrobial peptides human beta-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cells. J Immunol. 184 (7): 3526-3534.","DOI":"10.4049\/jimmunol.0900712"},{"key":"1406_CR12","doi-asserted-by":"publisher","first-page":"290","DOI":"10.2174\/187152109789760225","volume":"8","author":"J Pollard","year":"2009","unstructured":"Pollard J, Wright J, Feng Y, Geng D, Genberg C, Savage PB: Activities of Ceragenin CSA-13 Against Established Biofilms in an In Vitro Model of Catheter Decolonization. Anti-Infective Agents in Medicinal Chemistry. 2009, 8: 290-294.","journal-title":"Anti-Infective Agents in Medicinal Chemistry"},{"key":"1406_CR13","volume-title":"J Appl Microbiol","author":"K Leszczynska","year":"2010","unstructured":"Leszczynska K, Namiot A, Cruz K, Byfield FJ, Won E, Mendez G, Sokolowski W, Savage PB, Bucki R, Janmey PA: Potential of ceragenin CSA-13 and its mixture with pluronic F-127 as treatment of topical bacterial infections. J Appl Microbiol. 2010"},{"issue":"11","key":"1406_CR14","doi-asserted-by":"publisher","first-page":"4125","DOI":"10.1128\/AAC.00208-07","volume":"51","author":"N Beckloff","year":"2007","unstructured":"Beckloff N, Laube D, Castro T, Furgang D, Park S, Perlin D, Clements D, Tang H, Scott RW, Tew GN, et al: Activity of an antimicrobial peptide mimetic against planktonic and biofilm cultures of oral pathogens. Antimicrob Agents Chemother. 2007, 51 (11): 4125-4132. 10.1128\/AAC.00208-07.","journal-title":"Antimicrob Agents Chemother"},{"issue":"9","key":"1406_CR15","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1177\/039139881003300904","volume":"33","author":"F Lopez-Leban","year":"2010","unstructured":"Lopez-Leban F, Kiran MD, Wolcott R, Balaban N: Molecular mechanisms of RIP, an effective inhibitor of chronic infections. Int J Artif Organs. 2010, 33 (9): 582-589.","journal-title":"Int J Artif Organs"},{"issue":"4","key":"1406_CR16","first-page":"343","volume":"34","author":"T Ganz","year":"1997","unstructured":"Ganz T, Weiss J: Antimicrobial peptides of phagocytes and epithelia. Seminars in hematology. 1997, 34 (4): 343-354.","journal-title":"Seminars in hematology"},{"issue":"5","key":"1406_CR17","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1189\/jlb.69.5.691","volume":"69","author":"D Yang","year":"2001","unstructured":"Yang D, Chertov O, Oppenheim JJ: Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). Journal of leukocyte biology. 2001, 69 (5): 691-697.","journal-title":"Journal of leukocyte biology"},{"issue":"2","key":"1406_CR18","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1016\/S0304-4165(98)00087-7","volume":"1425","author":"R Gennaro","year":"1998","unstructured":"Gennaro R, Scocchi M, Merluzzi L, Zanetti M: Biological characterization of a novel mammalian antimicrobial peptide. Biochimica et biophysica acta. 1998, 1425 (2): 361-368.","journal-title":"Biochimica et biophysica acta"},{"issue":"5","key":"1406_CR19","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1080\/02713680590934111","volume":"30","author":"YJ Gordon","year":"2005","unstructured":"Gordon YJ, Huang LC, Romanowski EG, Yates KA, Proske RJ, McDermott AM: Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity. Curr Eye Res. 2005, 30 (5): 385-394. 10.1080\/02713680590934111.","journal-title":"Curr Eye Res"},{"issue":"8","key":"1406_CR20","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1097\/00029330-200704020-00018","volume":"120","author":"LG Si","year":"2007","unstructured":"Si LG, Liu XC, Lu YY, Wang GY, Li WM: Soluble expression of active human beta-defensin-3 in Escherichia coli and its effects on the growth of host cells. Chinese medical journal. 2007, 120 (8): 708-713.","journal-title":"Chinese medical journal"},{"issue":"9","key":"1406_CR21","doi-asserted-by":"publisher","first-page":"e3217","DOI":"10.1371\/journal.pone.0003217","volume":"3","author":"Y Wang","year":"2008","unstructured":"Wang Y, Hong J, Liu X, Yang H, Liu R, Wu J, Wang A, Lin D, Lai R: Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. PLoS One. 2008, 3 (9): e3217-10.1371\/journal.pone.0003217.","journal-title":"PLoS One"},{"issue":"6","key":"1406_CR22","doi-asserted-by":"publisher","first-page":"1266","DOI":"10.1093\/jac\/dkn106","volume":"61","author":"K Ouhara","year":"2008","unstructured":"Ouhara K, Komatsuzawa H, Kawai T, Nishi H, Fujiwara T, Fujiue Y, Kuwabara M, Sayama K, Hashimoto K, Sugai M: Increased resistance to cationic antimicrobial peptide LL-37 in methicillin-resistant strains of Staphylococcus aureus. The Journal of antimicrobial chemotherapy. 2008, 61 (6): 1266-1269. 10.1093\/jac\/dkn106.","journal-title":"The Journal of antimicrobial chemotherapy"},{"issue":"12","key":"1406_CR23","doi-asserted-by":"publisher","first-page":"4761","DOI":"10.1073\/pnas.87.12.4761","volume":"87","author":"D Wade","year":"1990","unstructured":"Wade D, Boman A, Wahlin B, Drain CM, Andreu D, Boman HG, Merrifield RB: All-D amino acid-containing channel-forming antibiotic peptides. Proc Natl Acad Sci USA. 1990, 87 (12): 4761-4765. 10.1073\/pnas.87.12.4761.","journal-title":"Proc Natl Acad Sci USA"},{"issue":"10","key":"1406_CR24","doi-asserted-by":"publisher","first-page":"1685","DOI":"10.1016\/j.peptides.2008.06.008","volume":"29","author":"H Zhao","year":"2008","unstructured":"Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y: Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides. 2008, 29 (10): 1685-1691. 10.1016\/j.peptides.2008.06.008.","journal-title":"Peptides"},{"issue":"2","key":"1406_CR25","doi-asserted-by":"publisher","first-page":"246","DOI":"10.1016\/j.bbrc.2010.04.073","volume":"396","author":"LS Amer","year":"2010","unstructured":"Amer LS, Bishop BM, van Hoek ML: Antimicrobial and antibiofilm activity of cathelicidins and short, synthetic peptides against Francisella. Biochem Biophys Res Commun. 2010, 396 (2): 246-251. 10.1016\/j.bbrc.2010.04.073.","journal-title":"Biochem Biophys Res Commun"},{"issue":"4","key":"1406_CR26","doi-asserted-by":"publisher","first-page":"825","DOI":"10.1016\/j.bbrc.2010.04.158","volume":"396","author":"FA de Latour","year":"2010","unstructured":"de Latour FA, Amer LS, Papanstasiou EA, Bishop BM, van Hoek ML: Antimicrobial activity of the Naja atra cathelicidin and related small peptides. Biochem Biophys Res Commun. 2010, 396 (4): 825-830. 10.1016\/j.bbrc.2010.04.158.","journal-title":"Biochem Biophys Res Commun"},{"issue":"1-2","key":"1406_CR27","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/S0022-1759(97)00084-7","volume":"206","author":"O Sorensen","year":"1997","unstructured":"Sorensen O, Cowland JB, Askaa J, Borregaard N: An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma. J Immunol Methods. 1997, 206 (1-2): 53-59. 10.1016\/S0022-1759(97)00084-7.","journal-title":"J Immunol Methods"},{"issue":"10","key":"1406_CR28","doi-asserted-by":"publisher","first-page":"6771","DOI":"10.1128\/IAI.73.10.6771-6781.2005","volume":"73","author":"MH Braff","year":"2005","unstructured":"Braff MH, Zaiou M, Fierer J, Nizet V, Gallo RL: Keratinocyte production of cathelicidin provides direct activity against bacterial skin pathogens. Infection and immunity. 2005, 73 (10): 6771-6781. 10.1128\/IAI.73.10.6771-6781.2005.","journal-title":"Infection and immunity"},{"issue":"7","key":"1406_CR29","doi-asserted-by":"publisher","first-page":"492","DOI":"10.1111\/j.1600-0463.2009.02460.x","volume":"117","author":"EA Papanastasiou","year":"2009","unstructured":"Papanastasiou EA, Hua Q, Sandouk A, Son UH, Christenson AJ, Van Hoek ML, Bishop BM: Role of acetylation and charge in antimicrobial peptides based on human beta-defensin-3. Apmis. 2009, 117 (7): 492-499. 10.1111\/j.1600-0463.2009.02460.x.","journal-title":"Apmis"},{"issue":"11","key":"1406_CR30","doi-asserted-by":"publisher","first-page":"1741","DOI":"10.1016\/j.peptides.2003.07.026","volume":"24","author":"DL Cox","year":"2003","unstructured":"Cox DL, Sun Y, Liu H, Lehrer RI, Shafer WM: Susceptibility of Treponema pallidum to host-derived antimicrobial peptides. Peptides. 2003, 24 (11): 1741-1746. 10.1016\/j.peptides.2003.07.026.","journal-title":"Peptides"},{"issue":"5","key":"1406_CR31","doi-asserted-by":"publisher","first-page":"2748","DOI":"10.1128\/IAI.68.5.2748-2755.2000","volume":"68","author":"SM Travis","year":"2000","unstructured":"Travis SM, Anderson NN, Forsyth WR, Espiritu C, Conway BD, Greenberg EP, McCray PB, Lehrer RI, Welsh MJ, Tack BF: Bactericidal activity of mammalian cathelicidin-derived peptides. Infect Immun. 2000, 68 (5): 2748-2755. 10.1128\/IAI.68.5.2748-2755.2000.","journal-title":"Infect Immun"},{"issue":"9","key":"1406_CR32","doi-asserted-by":"publisher","first-page":"4176","DOI":"10.1128\/IAI.00318-08","volume":"76","author":"J Overhage","year":"2008","unstructured":"Overhage J, Campisano A, Bains M, Torfs EC, Rehm BH, Hancock RE: Human host defense peptide LL-37 prevents bacterial biofilm formation. Infect Immun. 2008, 76 (9): 4176-4182. 10.1128\/IAI.00318-08.","journal-title":"Infect Immun"},{"issue":"2","key":"1406_CR33","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1111\/j.1472-765X.2009.02778.x","volume":"50","author":"E Hell","year":"2010","unstructured":"Hell E, Giske CG, Nelson A, Romling U, Marchini G: Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis. Lett Appl Microbiol. 2010, 50 (2): 211-215. 10.1111\/j.1472-765X.2009.02778.x.","journal-title":"Lett Appl Microbiol"},{"issue":"3","key":"1406_CR34","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1016\/j.bbrc.2003.08.043","volume":"309","author":"KH Lee","year":"2003","unstructured":"Lee KH, Shin SY, Hong JE, Yang ST, Kim JI, Hahm KS, Kim Y: Solution structure of termite-derived antimicrobial peptide, spinigerin, as determined in SDS micelle by NMR spectroscopy. Biochemical and biophysical research communications. 2003, 309 (3): 591-597. 10.1016\/j.bbrc.2003.08.043.","journal-title":"Biochemical and biophysical research communications"},{"key":"1406_CR35","doi-asserted-by":"publisher","first-page":"13896","DOI":"10.1074\/jbc.M311418200","volume":"279","author":"IY Park","year":"2004","unstructured":"Park IY, Cho JH, Kim KS, Kim YB, Kim YS, Kim SC: Helix stability confers salt resistance upon helical antimicrobial peptides. J Biol Chem. 2004, 279: 13896-13901. 10.1074\/jbc.M311418200.","journal-title":"J Biol Chem"},{"issue":"4","key":"1406_CR36","doi-asserted-by":"publisher","first-page":"1181","DOI":"10.1046\/j.0014-2956.2002.02751.x","volume":"269","author":"BF Tack","year":"2002","unstructured":"Tack BF, Sawai MV, Kearney WR, Robertson AD, Sherman MA, Wang W, Hong T, Boo LM, Wu H, Waring AJ, et al: SMAP-29 has two LPS-binding sites and a central hinge. Eur J Biochem. 2002, 269 (4): 1181-1189. 10.1046\/j.0014-2956.2002.02751.x.","journal-title":"Eur J Biochem"},{"issue":"47","key":"1406_CR37","doi-asserted-by":"publisher","first-page":"32637","DOI":"10.1074\/jbc.M805533200","volume":"283","author":"G Wang","year":"2008","unstructured":"Wang G: Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem. 2008, 283 (47): 32637-32643. 10.1074\/jbc.M805533200.","journal-title":"J Biol Chem"},{"key":"1406_CR38","doi-asserted-by":"crossref","unstructured":"Patel R: Biofilms and antimicrobial resistance. Clinical orthopaedics and related research. 2005, 41-47. 437","DOI":"10.1097\/01.blo.0000175714.68624.74"},{"issue":"11","key":"1406_CR39","doi-asserted-by":"publisher","first-page":"6339","DOI":"10.1128\/IAI.70.11.6339-6345.2002","volume":"70","author":"JG Leid","year":"2002","unstructured":"Leid JG, Shirtliff ME, Costerton JW, Stoodley P: Human leukocytes adhere to, penetrate, and respond to Staphylococcus aureus biofilms. Infection and immunity. 2002, 70 (11): 6339-6345. 10.1128\/IAI.70.11.6339-6345.2002.","journal-title":"Infection and immunity"},{"issue":"2","key":"1406_CR40","doi-asserted-by":"publisher","first-page":"310","DOI":"10.1128\/MMBR.00041-08","volume":"73","author":"E Karatan","year":"2009","unstructured":"Karatan E, Watnick P: Signals, regulatory networks, and materials that build and break bacterial biofilms. Microbiol Mol Biol Rev. 2009, 73 (2): 310-347. 10.1128\/MMBR.00041-08.","journal-title":"Microbiol Mol Biol Rev"},{"issue":"29","key":"1406_CR41","doi-asserted-by":"publisher","first-page":"18586","DOI":"10.1074\/jbc.273.29.18586","volume":"273","author":"C Gerke","year":"1998","unstructured":"Gerke C, Kraft A, Sussmuth R, Schweitzer O, Gotz F: Characterization of the N-acetylglucosaminyltransferase activity involved in the biosynthesis of the Staphylococcus epidermidis polysaccharide intercellular adhesin. J Biol Chem. 1998, 273 (29): 18586-18593. 10.1074\/jbc.273.29.18586.","journal-title":"J Biol Chem"},{"issue":"2","key":"1406_CR42","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1128\/AEM.02073-07","volume":"74","author":"EA Izano","year":"2008","unstructured":"Izano EA, Amarante MA, Kher WB, Kaplan JB: Differential roles of poly-N-acetylglucosamine surface polysaccharide and extracellular DNA in Staphylococcus aureus and Staphylococcus epidermidis biofilms. Appl Environ Microbiol. 2008, 74 (2): 470-476. 10.1128\/AEM.02073-07.","journal-title":"Appl Environ Microbiol"},{"issue":"3","key":"1406_CR43","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1046\/j.1523-1747.2003.12069.x","volume":"120","author":"JD Heilborn","year":"2003","unstructured":"Heilborn JD, Nilsson MF, Kratz G, Weber G, Sorensen O, Borregaard N, Stahle-Backdahl M: The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J Invest Dermatol. 2003, 120 (3): 379-389. 10.1046\/j.1523-1747.2003.12069.x.","journal-title":"J Invest Dermatol"},{"issue":"4","key":"1406_CR44","doi-asserted-by":"publisher","first-page":"2688","DOI":"10.4049\/jimmunol.0802586","volume":"183","author":"N Mookherjee","year":"2009","unstructured":"Mookherjee N, Lippert DN, Hamill P, Falsafi R, Nijnik A, Kindrachuk J, Pistolic J, Gardy J, Miri P, Naseer M, et al: Intracellular receptor for human host defense peptide LL-37 in monocytes. J Immunol. 2009, 183 (4): 2688-2696. 10.4049\/jimmunol.0802586.","journal-title":"J Immunol"},{"issue":"7","key":"1406_CR45","doi-asserted-by":"publisher","first-page":"4662","DOI":"10.4049\/jimmunol.175.7.4662","volume":"175","author":"S Tokumaru","year":"2005","unstructured":"Tokumaru S, Sayama K, Shirakata Y, Komatsuzawa H, Ouhara K, Hanakawa Y, Yahata Y, Dai X, Tohyama M, Nagai H, et al: Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37. J Immunol. 2005, 175 (7): 4662-4668.","journal-title":"J Immunol"},{"issue":"12","key":"1406_CR46","doi-asserted-by":"publisher","first-page":"6690","DOI":"10.4049\/jimmunol.171.12.6690","volume":"171","author":"GS Tjabringa","year":"2003","unstructured":"Tjabringa GS, Aarbiou J, Ninaber DK, Drijfhout JW, Sorensen OE, Borregaard N, Rabe KF, Hiemstra PS: The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J Immunol. 2003, 171 (12): 6690-6696.","journal-title":"J Immunol"},{"issue":"45","key":"1406_CR47","doi-asserted-by":"publisher","first-page":"30471","DOI":"10.1074\/jbc.M802185200","volume":"283","author":"L Tomasinsig","year":"2008","unstructured":"Tomasinsig L, Pizzirani C, Skerlavaj B, Pellegatti P, Gulinelli S, Tossi A, Di Virgilio F, Zanetti M: The human cathelicidin LL-37 modulates the activities of the P2X7 receptor in a structure-dependent manner. J Biol Chem. 2008, 283 (45): 30471-30481. 10.1074\/jbc.M802185200.","journal-title":"J Biol Chem"},{"key":"1406_CR48","doi-asserted-by":"crossref","unstructured":"Durham-Colleran MW, Verhoeven AB, van Hoek ML: Francisella novicida forms in vitro biofilms mediated by an orphan response regulator. Microbial ecology. 59 (3): 457-465.","DOI":"10.1007\/s00248-009-9586-9"}],"container-title":["BMC Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/1471-2180-11-114.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,6,7]],"date-time":"2023-06-07T00:00:37Z","timestamp":1686096037000},"score":1,"resource":{"primary":{"URL":"https:\/\/bmcmicrobiol.biomedcentral.com\/articles\/10.1186\/1471-2180-11-114"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,5,23]]},"references-count":48,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2011,12]]}},"alternative-id":["1406"],"URL":"https:\/\/doi.org\/10.1186\/1471-2180-11-114","relation":{},"ISSN":["1471-2180"],"issn-type":[{"value":"1471-2180","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,5,23]]},"assertion":[{"value":"7 January 2011","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 May 2011","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 May 2011","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}],"article-number":"114"}}