Inhibition of Listeria monocytogenes by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles

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dc.citation.issue6
dc.citation.volume11
dc.contributor.authorStone E
dc.contributor.authorPennone V
dc.contributor.authorReilly K
dc.contributor.authorGrant IR
dc.contributor.authorCampbell K
dc.contributor.authorAltermann E
dc.contributor.authorMcAuliffe O
dc.coverage.spatialSwitzerland
dc.date.accessioned2024-06-12T20:53:58Z
dc.date.available2024-06-12T20:53:58Z
dc.date.issued2022-03-17
dc.description.abstractThe high mortality rate associated with Listeria monocytogenes 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 L. monocytogenes. Turbidity reduction assays confirmed the lysis of L. monocytogenes cells at 37 °C upon addition of the tailored BNPs. The application of BNPs also resulted in the growth inhibition of L. monocytogenes. BNPs displaying only the amidase domain of the phage endolysin were more effective at inhibiting growth under laboratory conditions (37 °C, 3 × 107 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 × 103 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 L. monocytogenes.
dc.description.confidentialfalse
dc.edition.editionMarch-2 2022
dc.format.pagination854-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/35327276
dc.identifier.citationStone E, Pennone V, Reilly K, Grant IR, Campbell K, Altermann E, McAuliffe O. (2022). Inhibition of Listeria monocytogenes by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles.. Foods. 11. 6. (pp. 854-).
dc.identifier.doi10.3390/foods11060854
dc.identifier.eissn2304-8158
dc.identifier.elements-typejournal-article
dc.identifier.issn2304-8158
dc.identifier.number854
dc.identifier.piifoods11060854
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/69815
dc.languageeng
dc.publisherMDPI (Basel, Switzerland)
dc.publisher.urihttps://www.mdpi.com/2304-8158/11/6/854
dc.relation.isPartOfFoods
dc.rights(c) 2022 The Author/s
dc.rightsCC BY 4.0
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectBNPs
dc.subjectListeria monocytogenes
dc.subjectamidase
dc.subjectbacteriophage
dc.subjectbionanoparticles
dc.subjectendolysin
dc.titleInhibition of Listeria monocytogenes by Phage Lytic Enzymes Displayed on Tailored Bionanoparticles
dc.typeJournal article
pubs.elements-id486129
pubs.organisational-groupOther
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