Journal
ISCIENCE
Volume 23, Issue 8, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.isci.2020.101423
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Funding
- UK's Department for Business, Energy and Industrial Strategy
- Innovate UK [103358]
- UK's Biotechnology and Biological Sciences Council (BBSRC) [BB/N015487/1, BB/J021474/1, MR/R000328/1]
- UK's Medical Research Council (MRC) [BB/N015487/1, BB/J021474/1, MR/R000328/1]
- BBSRC [BB/J021474/1, BB/M01830X/1, BB/N015487/1] Funding Source: UKRI
- EPSRC [EP/M028100/1] Funding Source: UKRI
- Innovate UK [103358] Funding Source: UKRI
- MRC [MR/R000328/1] Funding Source: UKRI
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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 antibac-terial 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 relation-ships in pore-forming proteins.
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