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http://purl.uniprot.org/citations/32795916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32795916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32795916http://www.w3.org/2000/01/rdf-schema#comment"Bacteriocins are a distinct family of antimicrobial proteins postulated to porate bacterial membranes. However, direct experimental evidence of pore formation by these proteins is lacking. Here we report a multi-mode poration mechanism induced by four-helix bacteriocins, epidermicin NI01 and aureocin A53. Using a combination of crystallography, spectroscopy, bioassays, and nanoscale imaging, we established that individual two-helix segments of epidermicin retain antibacterial activity but each of these segments adopts a particular poration mode. In the intact protein these segments act synergistically to balance out antibacterial and hemolytic activities. The study sets a precedent of multi-mode membrane disruption advancing the current understanding of structure-activity relationships in pore-forming proteins."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.org/dc/terms/identifier"doi:10.1016/j.isci.2020.101423"xsd:string
http://purl.uniprot.org/citations/32795916http://purl.org/dc/terms/identifier"doi:10.1016/j.isci.2020.101423"xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Derrick J.P."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Derrick J.P."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Ravi J."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Ravi J."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Upton M."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Upton M."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Lewis H."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Lewis H."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Hoogenboom B.W."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Hoogenboom B.W."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Desriac F."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Desriac F."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Halliwell S."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Halliwell S."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Hammond K."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Hammond K."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Nardone B."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Nardone B."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Ryadnov M.G."xsd:string
http://purl.uniprot.org/citations/32795916http://purl.uniprot.org/core/author"Ryadnov M.G."xsd:string