Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles
The high mortality rate associated with <i>Listeria monocytogenes</i> and its ability to adapt to the harsh conditions employed in food processing has ensured that this pathogen remains a serious problem in the ready-to-eat food sector. Bacteriophage-derived enzymes can be applied as bio...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/6/854 |
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| author | Edel Stone Vincenzo Pennone Kerri Reilly Irene R. Grant Katrina Campbell Eric Altermann Olivia McAuliffe |
| author_facet | Edel Stone Vincenzo Pennone Kerri Reilly Irene R. Grant Katrina Campbell Eric Altermann Olivia McAuliffe |
| author_sort | Edel Stone |
| collection | DOAJ |
| description | The high mortality rate associated with <i>Listeria monocytogenes</i> and its ability to adapt to the harsh conditions employed in food processing has ensured that this pathogen remains a serious problem in the ready-to-eat food sector. Bacteriophage-derived enzymes can be applied as biocontrol agents to target specific foodborne pathogens. We investigated the ability of a listeriophage endolysin and derivatives thereof, fused to polyhydroxyalkanoate bionanoparticles (PHA_BNPs), to lyse and inhibit the growth of <i>L. monocytogenes</i>. Turbidity reduction assays confirmed the lysis of <i>L. monocytogenes</i> cells at 37 °C upon addition of the tailored BNPs. The application of BNPs also resulted in the growth inhibition of <i>L. monocytogenes.</i> BNPs displaying only the amidase domain of the phage endolysin were more effective at inhibiting growth under laboratory conditions (37 °C, 3 × 10<sup>7</sup> CFU/mL) than BNPs displaying the full-length endolysin (89% vs. 83% inhibition). Under conditions that better represent those found in food processing environments (22 °C, 1 × 10<sup>3</sup> CFU/mL), BNPs displaying the full-length endolysin demonstrated a greater inhibitory effect compared to BNPs displaying only the amidase domain (61% vs. 54% inhibition). Our results demonstrate proof-of-concept that tailored BNPs displaying recombinant listeriophage enzymes are active inhibitors of <i>L. monocytogenes</i>. |
| first_indexed | 2024-03-09T19:51:45Z |
| format | Article |
| id | doaj.art-f5ffb39784b4441d9f40284e7fbeabf8 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T19:51:45Z |
| publishDate | 2022-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-f5ffb39784b4441d9f40284e7fbeabf82023-11-24T01:10:56ZengMDPI AGFoods2304-81582022-03-0111685410.3390/foods11060854Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored BionanoparticlesEdel Stone0Vincenzo Pennone1Kerri Reilly2Irene R. Grant3Katrina Campbell4Eric Altermann5Olivia McAuliffe6Teagasc Food Research Centre, Moorepark, Fermoy, P61 C996 Cork, IrelandTeagasc Food Research Centre, Moorepark, Fermoy, P61 C996 Cork, IrelandAgResearch Ltd., Palmerston North 4410, New ZealandInstitute for Global Food Security, School of Biological Sciences, Queens University, 19 Chlorine Gardens, BT9 5DL Belfast, IrelandInstitute for Global Food Security, School of Biological Sciences, Queens University, 19 Chlorine Gardens, BT9 5DL Belfast, IrelandAgResearch Ltd., Palmerston North 4410, New ZealandTeagasc Food Research Centre, Moorepark, Fermoy, P61 C996 Cork, IrelandThe high mortality rate associated with <i>Listeria monocytogenes</i> and its ability to adapt to the harsh conditions employed in food processing has ensured that this pathogen remains a serious problem in the ready-to-eat food sector. Bacteriophage-derived enzymes can be applied as biocontrol agents to target specific foodborne pathogens. We investigated the ability of a listeriophage endolysin and derivatives thereof, fused to polyhydroxyalkanoate bionanoparticles (PHA_BNPs), to lyse and inhibit the growth of <i>L. monocytogenes</i>. Turbidity reduction assays confirmed the lysis of <i>L. monocytogenes</i> cells at 37 °C upon addition of the tailored BNPs. The application of BNPs also resulted in the growth inhibition of <i>L. monocytogenes.</i> BNPs displaying only the amidase domain of the phage endolysin were more effective at inhibiting growth under laboratory conditions (37 °C, 3 × 10<sup>7</sup> CFU/mL) than BNPs displaying the full-length endolysin (89% vs. 83% inhibition). Under conditions that better represent those found in food processing environments (22 °C, 1 × 10<sup>3</sup> CFU/mL), BNPs displaying the full-length endolysin demonstrated a greater inhibitory effect compared to BNPs displaying only the amidase domain (61% vs. 54% inhibition). Our results demonstrate proof-of-concept that tailored BNPs displaying recombinant listeriophage enzymes are active inhibitors of <i>L. monocytogenes</i>.https://www.mdpi.com/2304-8158/11/6/854<i>Listeria monocytogenes</i>bacteriophageendolysinamidasebionanoparticlesBNPs |
| spellingShingle | Edel Stone Vincenzo Pennone Kerri Reilly Irene R. Grant Katrina Campbell Eric Altermann Olivia McAuliffe Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles Foods <i>Listeria monocytogenes</i> bacteriophage endolysin amidase bionanoparticles BNPs |
| title | Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles |
| title_full | Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles |
| title_fullStr | Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles |
| title_full_unstemmed | Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles |
| title_short | Inhibition of <i>Listeria monocytogenes</i> by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles |
| title_sort | inhibition of i listeria monocytogenes i by phage lytic enzymes displayed on tailored bionanoparticles |
| topic | <i>Listeria monocytogenes</i> bacteriophage endolysin amidase bionanoparticles BNPs |
| url | https://www.mdpi.com/2304-8158/11/6/854 |
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