Flowering Poration—A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold
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 aureoci...
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Veröffentlicht in: | iScience 2020-08, Vol.23 (8), p.101423-101423, Article 101423 |
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Sprache: | eng |
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Zusammenfassung: | 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.
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•Bacteriocins are antibacterial proteins believed to form pores in bacterial membranes•A multi-helix bacteriocin fold induces a multi-mode poration mechanism•Each of two-helix segments of the bacteriocin adopts a particular poration mode•These segments act synergistically balancing out antibacterial and hemolytic activities
Biological Sciences; Microbiology; Structural Biology |
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ISSN: | 2589-0042 2589-0042 |
DOI: | 10.1016/j.isci.2020.101423 |