| Autor: |
Larpin Y; Institute of Anatomy, University of Bern, 3012 Bern, Switzerland., Besançon H; Institute of Anatomy, University of Bern, 3012 Bern, Switzerland., Babiychuk VS; Institute of Anatomy, University of Bern, 3012 Bern, Switzerland., Babiychuk EB; Institute of Anatomy, University of Bern, 3012 Bern, Switzerland., Köffel R; Institute of Anatomy, University of Bern, 3012 Bern, Switzerland. |
| Jazyk: |
angličtina |
| Zdroj: |
Toxins [Toxins (Basel)] 2021 Feb 09; Vol. 13 (2). Date of Electronic Publication: 2021 Feb 09. |
| DOI: |
10.3390/toxins13020126 |
| Abstrakt: |
Pore-forming toxins (PFTs) form multimeric trans-membrane pores in cell membranes that differ in pore channel diameter (PCD). Cellular resistance to large PFTs (>20 nm PCD) was shown to rely on Ca 2+ influx activated membrane repair mechanisms. Small PFTs (<2 nm PCD) were shown to exhibit a high cytotoxic activity, but host cell response and membrane repair mechanisms are less well studied. We used monocytic immune cell lines to investigate the cellular resistance and host membrane repair mechanisms to small PFTs lysenin ( Eisenia fetida ) and aerolysin ( Aeromonas hydrophila ). Lysenin, but not aerolysin, is shown to induce Ca 2+ influx from the extracellular space and to activate Ca 2+ dependent membrane repair mechanisms. Moreover, lysenin binds to U937 cells with higher efficiency as compared to THP-1 cells, which is in line with a high sensitivity of U937 cells to lysenin. In contrast, aerolysin equally binds to U937 or THP-1 cells, but in different plasma membrane areas. Increased aerolysin induced cell death of U937 cells, as compared to THP-1 cells, is suggested to be a consequence of cap-like aerolysin binding. We conclude that host cell resistance to small PFTs attack comprises binding efficiency, pore localization, and capability to induce Ca 2+ dependent membrane repair mechanisms. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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