Next Article in Journal
A Combination of Real-Time PCR and High-Resolution Melting Analysis to Detect and Identify CpGV Genotypes Involved in Type I Resistance
Previous Article in Journal
Prevalence, Geographic Distribution, Risk Factors and Co-Infections of Feline Gammaherpesvirus Infections in Domestic Cats in Switzerland
Previous Article in Special Issue
Application of the Phage Lysin Ply5218 in the Treatment of Streptococcus suis Infection in Piglets
Open AccessArticle

Inhibition of L. monocytogenes Biofilm Formation by the Amidase Domain of the Phage vB_LmoS_293 Endolysin

1
Teagasc Food Research Center, Moorepark, Fermoy, Co. Cork P61 C996, Ireland
2
Centro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain
3
Cork Institute of Technology, Bishopstown, Cork T12 P928, Ireland
*
Author to whom correspondence should be addressed.
Viruses 2019, 11(8), 722; https://doi.org/10.3390/v11080722
Received: 26 March 2019 / Revised: 1 August 2019 / Accepted: 2 August 2019 / Published: 6 August 2019
Listeria monocytogenes is a ubiquitous Gram-positive bacterium that is a major concern for food business operators because of its pathogenicity and ability to form biofilms in food production environments. Bacteriophages (phages) have been evaluated as biocontrol agents for L. monocytogenes in a number of studies and, indeed, certain phages have been approved for use as anti-listerial agents in food processing environments (ListShield and PhageGuard Listex). Endolysins are proteins produced by phages in the host cell. They cleave the peptidoglycan cell wall, thus allowing release of progeny phage into the environment. In this study, the amidase domain of the phage vB_LmoS_293 endolysin (293-amidase) was cloned and expressed in Escherichia. coli (E. coli). Muralytic activity at different concentrations, pH and temperature values, lytic spectrum and activity against biofilms was determined for the purified 293-amidase protein. The results showed activity on autoclaved cells at three different temperatures (20 °C, 37 °C and 50 °C), with a wider specificity (L. monocytogenes 473 and 3099, a serotype 4b and serogroup 1/2b-3b-7, respectively) compared to the phage itself, which targets only L. monocytogenes serotypes 4b and 4e. The protein also inhibits biofilm formation on abiotic surfaces. These results show the potential of using recombinant antimicrobial proteins against pathogens in the food production environment. View Full-Text
Keywords: listeriophage; endolysin; amidase listeriophage; endolysin; amidase
Show Figures

Graphical abstract

MDPI and ACS Style

Pennone, V.; Sanz-Gaitero, M.; O’Connor, P.; Coffey, A.; Jordan, K.; van Raaij, M.J.; McAuliffe, O. Inhibition of L. monocytogenes Biofilm Formation by the Amidase Domain of the Phage vB_LmoS_293 Endolysin. Viruses 2019, 11, 722.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map

1
Back to TopTop