{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:30:55Z","timestamp":1791307855493,"version":"4.3.1"},"reference-count":55,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2007,2,15]]},"abstract":"<jats:p>We have isolated and characterized omwaprin, a 50-amino-acid cationic protein from the venom of inland taipan (Oxyuranus microlepidotus). It is a new member of the waprin family of snake venom proteins. A synthetic gene was designed and constructed for expressing the recombinant protein in Escherichia coli. Recombinant omwaprin was used for carrying out functional analyses. The protein is non-toxic to Swiss albino mice at doses of up to 10\u00a0mg\/kg when administered intraperitoneally. However, it shows selective and dose-dependant antibacterial activity against Gram-positive bacteria. The minimum inhibitory doses were in the range 2\u201310\u00a0\u03bcg for selected species of bacteria in radial diffusion assays. The antibacterial activity is salt-tolerant up to 350\u00a0mM NaCl. However, omwaprin lost its antibacterial activity upon reduction and alkylation of its cysteine residues, or upon deletion of six N-terminal amino acid residues, four of which are positively charged. These observations indicate that the three-dimensional structure constrained by four disulfide bonds and the N-terminal residues are essential for its activity. The mechanism of action is via membrane disruption, as shown by scanning electron microscopy. Importantly, omwaprin lacks haemolytic activity on human erythrocytes. This demonstrates the specificity of omwaprin for bacterial membranes. Unlike other reported WAP (whey acidic protein) domain-containing antibacterial proteins, including elafin, EPPIN (epididymal proteinase inhibitor), SWAM1 and SWAM2 [single WAP (whey acidic protein) motif proteins 1 and 2] and SLPI (secretory leucocyte proteinase inhibitor), omwaprin shows species-specific activity on the Gram-positive bacteria tested.<\/jats:p>","DOI":"10.1042\/bj20060318","type":"journal-article","created":{"date-parts":[[2007,1,25]],"date-time":"2007-01-25T14:42:48Z","timestamp":1169736168000},"page":"93-104","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":138,"title":["Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins"],"prefix":"10.1042","volume":"402","author":[{"given":"Dileep\u00a0G.","family":"Nair","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117543"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bryan\u00a0G.","family":"Fry","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117543"},{"name":"Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia 4072"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul","family":"Alewood","sequence":"additional","affiliation":[{"name":"Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia 4072"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prakash\u00a0P.","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117543"},{"name":"Temasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore 117604"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R.\u00a0Manjunatha","family":"Kini","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 117543"},{"name":"Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, Richmond, VA 23298, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2007,1,25]]},"reference":[{"key":"2021112213070159200_B1","doi-asserted-by":"crossref","first-page":"2583","DOI":"10.1021\/bi00815a005","article-title":"Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom","volume":"9","author":"Ferreira","year":"1970","journal-title":"Biochemistry"},{"key":"2021112213070159200_B2","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1097\/00001721-199807000-00001","article-title":"Use of snake venom fractions in the coagulation laboratory","volume":"9","author":"Marsh","year":"1998","journal-title":"Blood Coagulation Fibrinolysis"},{"key":"2021112213070159200_B3","first-page":"211","article-title":"Diagnostic uses of snake venom","volume":"31","author":"Marsh","year":"2001","journal-title":"Haemostasis"},{"key":"2021112213070159200_B4","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1093\/ecam\/neh063","article-title":"Snake venom: any clue for antibiotics and CAM?","volume":"2","author":"de\u00a0Lima","year":"2005","journal-title":"Evidence-Based Complement Altern. 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