{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T20:46:45Z","timestamp":1790455605320,"version":"4.1.0"},"reference-count":51,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2012,3,1]],"date-time":"2012-03-01T00:00:00Z","timestamp":1330560000000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2012,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    We describe the discovery, purification, characterization, and expression of an antimicrobial peptide, epidermicin NI01, which is an unmodified bacteriocin produced by\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Staphylococcus epidermidis<\/jats:named-content>\n                    strain 224. It is a highly cationic, hydrophobic, plasmid-encoded peptide that exhibits potent antimicrobial activity toward a wide range of pathogenic Gram-positive bacteria including methicillin-resistant\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Staphylococcus aureus<\/jats:named-content>\n                    (MRSA), enterococci, and biofilm-forming\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. epidermidis<\/jats:named-content>\n                    strains. Purification of the peptide was achieved using a combination of hydrophobic interaction, cation exchange, and high-performance liquid chromatography (HPLC). Matrix-assisted laser desorption ionization\u2013time of flight (MALDI-TOF) analysis yielded a molecular mass of 6,074 Da, and partial sequence data of the peptide were elucidated using a combination of tandem mass spectrometry (MS\/MS) and\n                    <jats:italic>de novo<\/jats:italic>\n                    sequencing. The draft genome sequence of the producing strain was obtained using 454 pyrosequencing technology, thus enabling the identification of the structural gene using the\n                    <jats:italic>de novo<\/jats:italic>\n                    peptide sequence data previously obtained. Epidermicin NI01 contains 51 residues with four tryptophan and nine lysine residues, and the sequence showed approximately 50% identity to peptides lacticin Z, lacticin Q, and aureocin A53, all of which belong to a new family of unmodified type II-like bacteriocins. The peptide is active in the nanomolar range against\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. epidermidis<\/jats:named-content>\n                    , MRSA isolates, and vancomycin-resistant enterococci. Other unique features displayed by epidermicin include a high degree of protease stability and the ability to retain antimicrobial activity over a pH range of 2 to 10, and exposure to the peptide does not result in development of resistance in susceptible isolates. In this study we also show the structural gene alone can be cloned into\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n                    strain BL21(DE3), and expression yields active peptide.\n                  <\/jats:p>","DOI":"10.1128\/aac.05397-11","type":"journal-article","created":{"date-parts":[[2011,12,13]],"date-time":"2011-12-13T00:21:18Z","timestamp":1323735678000},"page":"1539-1547","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":118,"title":["Identification, Characterization, and Recombinant Expression of Epidermicin NI01, a Novel Unmodified Bacteriocin Produced by Staphylococcus epidermidis That Displays Potent Activity against Staphylococci"],"prefix":"10.1128","volume":"56","author":[{"given":"Stephanie","family":"Sandiford","sequence":"first","affiliation":[{"name":"Department of Medical Microbiology, School of Medicine, University of Manchester, Oxford Road, Manchester, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mathew","family":"Upton","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology, School of Medicine, University of Manchester, Oxford Road, Manchester, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1986.tb09933.x"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"38","DOI":"10.2174\/138920109787048580","article-title":"Staphylococcal antimicrobial peptides: relevant properties and potential biotechnological application","volume":"10","author":"Bastos MC","year":"2009","unstructured":"BastosMC CeottoH CoelhoML NascimentoJS. 2009. Staphylococcal antimicrobial peptides: relevant properties and potential biotechnological application. Curr. Pharm. Biotechnol. 10:38\u201361.","journal-title":"Curr. Pharm. Biotechnol"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1016\/j.peptides.2010.08.008","article-title":"Cost-effective expression and purification of antimicrobial and host defense peptides in Escherichia coli","volume":"31","author":"Bommarius B","year":"2010","unstructured":"BommariusB. 2010. Cost-effective expression and purification of antimicrobial and host defense peptides in Escherichia coli. 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