Please use this identifier to cite or link to this item: https://doi.org/10.1042/BJ20060318
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dc.titleAntimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins
dc.contributor.authorNair, D.G.
dc.contributor.authorFry, B.G.
dc.contributor.authorAlewood, P.
dc.contributor.authorKumar, P.P.
dc.contributor.authorKini, R.M.
dc.date.accessioned2014-10-27T08:21:59Z
dc.date.available2014-10-27T08:21:59Z
dc.date.issued2007-02-15
dc.identifier.citationNair, D.G., Fry, B.G., Alewood, P., Kumar, P.P., Kini, R.M. (2007-02-15). Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins. Biochemical Journal 402 (1) : 93-104. ScholarBank@NUS Repository. https://doi.org/10.1042/BJ20060318
dc.identifier.issn02646021
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100099
dc.description.abstractWe 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 mg/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 2-10 μg for selected species of bacteria in radial diffusion assays. The antibacterial activity is salt-tolerant up to 350 mM 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. © 2007 Biochemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1042/BJ20060318
dc.sourceScopus
dc.subjectAntibacterial protein
dc.subjectAntimicrobial protein
dc.subjectInland taipan (Oxyuranus microlepidotus)
dc.subjectOmwaprin
dc.subjectSnake venom
dc.subjectWAP domain (whey acidic protein domain)
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1042/BJ20060318
dc.description.sourcetitleBiochemical Journal
dc.description.volume402
dc.description.issue1
dc.description.page93-104
dc.description.codenBIJOA
dc.identifier.isiut000244284400010
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