This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by O'Flaherty, S. Articles by Ross, R. P. Search for Related Content PubMed PubMed Citation Articles by O'Flaherty, S. Articles by Ross, R. P.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2005, p. 7161-7164, Vol. 187, No. 20
0021-9193/05/$08.00+0     doi:10.1128/JB.187.20.7161-7164.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Recombinant Phage Lysin LysK Has a Broad Spectrum of Lytic Activity against Clinically Relevant Staphylococci, Including Methicillin-Resistant Staphylococcus aureus

Dairy Products Research Centre, Teagasc, Moorepark, Fermoy, Co. Cork, Ireland,¹ Dairy Production Research Centre, Teagasc, Moorepark, Fermoy, Co. Cork, Ireland,² Department of Microbiology, University College, Cork, Ireland,³ Department of Biological Sciences, Cork Institute of Technology, Bishopstown, Cork, Ireland,⁴ Alimentary Pharmabiotic Centre, Cork, Ireland⁵

Received 29 April 2005/ Accepted 30 July 2005

This study concerns the cloning, characterization, and expression of the lysin (LysK) from staphylococcal phage K in Lactococcus lactis. Lactococcal lysates containing recombinant LysK were found to inhibit a range of different species of staphylococci isolated from bovine and human infection sources, including methicillin-resistant Staphylococcus aureus. LysK thus has potential as an antimicrobial for applications in the prevention and/or treatment of infections caused by staphylococci.

This article has been cited by other articles:

• Mayer, M. J., Narbad, A., Gasson, M. J. (2008). Molecular Characterization of a Clostridium difficile Bacteriophage and Its Cloned Biologically Active Endolysin. J. Bacteriol. 190: 6734-6740 [Abstract] [Full Text]  
• Wegmann, U., O'Connell-Motherway, M., Zomer, A., Buist, G., Shearman, C., Canchaya, C., Ventura, M., Goesmann, A., Gasson, M. J., Kuipers, O. P., van Sinderen, D., Kok, J. (2007). Complete Genome Sequence of the Prototype Lactic Acid Bacterium Lactococcus lactis subsp. cremoris MG1363. J. Bacteriol. 189: 3256-3270 [Abstract] [Full Text]  
• Sass, P., Bierbaum, G. (2007). Lytic Activity of Recombinant Bacteriophage {phi}11 and {phi}12 Endolysins on Whole Cells and Biofilms of Staphylococcus aureus. Appl. Environ. Microbiol. 73: 347-352 [Abstract] [Full Text]  
• Borysowski, J., Weber-Dabrowska, B., Gorski, A. (2006). Bacteriophage endolysins as a novel class of antibacterial agents.. Exp. Biol. Med. 231: 366-377 [Abstract] [Full Text]