Determination of the mode of action of enterolysin A, produced by Enterococcus faecalis B9510

Journal of Applied Microbiology

Volumn 115, Issue 2, 2013, Pages 484-494

  Khan, H ^a   Flint, S H ^b   Yu, P L ^a  

^a MASSEY UNIVERSITY   (New Zealand)

^b MASSEY UNIVERSITY   (New Zealand)

Author keywords

Bacteriocin; Enterococcus faecalis; Enterolysin A; Mode of action; Transmission electron microscopy

Indexed keywords

AMINO ACIDS; BACILLI; CELL MEMBRANES; CYTOLOGY; ESCHERICHIA COLI; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; PEPTIDES; SILICA GEL; THIN LAYER CHROMATOGRAPHY;

'CURRENT; BACTERIAL CELLS; BACTERIOCINS; CELL WALLS; CLEAVAGE SITES; ENTEROCOCCUS FAECALIS; ENTEROLYSIN A; MODE OF ACTION; PEPTIDE BONDS; PEPTIDOGLYCANS;

LOCATION;

AMINO ACID; BACTERIOCIN; ENTEROLYSIN A; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

BACTERIUM; CHROMATOGRAPHY; CLEAVAGE; DAMAGE; PEPTIDE; PROTEIN; SILICA; SOLVENT; STRAIN; TRANSMISSION ELECTRON MICROSCOPY;

ARTICLE; BACTERIAL CELL WALL; BACTERIAL GENE; BACTERIAL STRAIN; BACTERIUM CULTURE; CELL KILLING; CYTOLYSIS; DERIVATIZATION; ENTEROCOCCUS FAECALIS; GENE AMPLIFICATION; LACTOBACILLUS DELBRUECKII; LACTOCOCCUS LACTIS; NONHUMAN; PEDIOCOCCUS PENTOSACEUS; PROTEIN PURIFICATION; THIN LAYER CHROMATOGRAPHY; TRANSMISSION ELECTRON MICROSCOPY;

BACTERIA (MICROORGANISMS); ENTEROCOCCUS FAECALIS; LACTOBACILLUS DELBRUECKII; LACTOCOCCUS LACTIS; PEDIOCOCCUS PENTOSACEUS; POSIBACTERIA;

EID: 84880576108     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/jam.12240     Document Type: Article

References (28)

1. Almeida, T., Brandao, A., Munoz-Atienza, E., Goncalves, A., Torres, C., Igrejas, G., Hernandez, P.E., Herranz, C. et al. (2011) Identification of bacteriocin genes in enterococci isolated from game animals and saltwater fish. J Food Protect 74, 1252-1260.
2. Bastos, M.C.F., Coutinho, B.G. and Coelho, M.L.V. (2010) Lysostaphin, a Staphylococcal bacteriolysin with potential clinical applications. Pharmaceuticals 3, 1139-1161.
3. Beukes, M., Bierbaum, G., Sahl, H.G. and Hastings, J.W. (2000) Purification and partial characterization of a murein hydrolase, millericin B, produced by Streptococcus milleri NMSCC 061. Appl Environ Microbiol 66, 23-28.
4. Cleveland, R.F., Holtje, J.V., Wicken, A.J., Tomasz, A., Daneo-Moore, L. and Shockman, G.D. (1975) Inhibition of bacterial wall lysins by lipoteichoic acids and related compounds. Biochem Biophys Res Commun 67, 1128-1135.
5. Gargis, S.R., Heath, H.E., Heath, L.S., LeBlanc, P.A., Simmonds, R.S., Abbott, B.D., Timkovich, R. and Sloan, G.L. (2009) Use of 4-sulfophenyl isothiocyanate labeling and mass spectrometry to determine the site of action of the streptococcolytic peptidoglycan hydrolase zoocin A. Appl Environ Microbiol 75, 72-77.
6. Ghuysen, J.M., Tripper, D.J. and Strominger, J.L. (1966) Enzymes that degrade cell walls. Methods Enzymol 8, 685-699.
7. Grundling, A. and Schneewind, O. (2006) Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus. J Bacteriol 188, 2463-2472.
8. Heng, N.C.K., Wescombe, P.A., Burton, J.P., Jack, R.W. and Tag, J.R. (2007). The diversity of bacteriocins in Gram-positive bacteria. In Bacteriocins, Ecology and Evolution ed. Riley, M.A. and Chavan, M.A. pp. 45-92. Berlin: Springer-Verlag.
9. Hickey, R., Twomey, D., Ross, R. and Hill, C. (2003) Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors. Microbiol 149, 655-664.
10. Kandler, O. (1970) Amino acid sequence of the murein and taxonomy of the genera Lactobacillus, Bifidobacterium, Leuconostoc and Pediococcus. Int J Syst Bacteriol 20, 491-507.
11. Khan, H., Flint, S.H. and Yu, P.L. (2013) Development of a chemically defined medium for the production of enterolysin A from Enterococcus faecalis B9510. J App Microbiol 114, 1092-1102.
12. Maliničová, L., Piknová, M., Pristaš, P. and Javorský, P. (2010). Peptidoglycan hydrolases as novel tool for anti-enterococcal therapy. In Current Research, Technology and Education Topics in Applied Microbiology and Microbial Biotechnology (Vol. 1). ed. Méndez-Vilas, A. pp. 463-472. Badajoz: Formatex Research Centre.
13. Nigutova, K., Morovsky, M., Pristas, P., Teather, R.M., Holo, H. and Javorsky, P. (2007) Production of enterolysin A by rumen Enterococcus faecalis strain and occurrence of enlA homologues among ruminal Gram-positive cocci. J Appl Microbiol 102, 563-569.
14. Nilsen, T., Nes, I.F. and Holo, H. (2003) Enterolysin A, a cell wall-degrading bacteriocin from Enterococcus faecalis LMG 2333. Appl Environ Microbiol 69, 2975-2984.
15. Nissen-Meyer, J., Holo, H., Havarstein, L.S., Sletten, K. and Nes, I.F. (1992) A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J Bacteriol 174, 5686-5692.
16. Pucciarelli, M., Bierne, H. and Portillo, F. (2007). The cell wall of Listeria monocytogenes and its role in pathogenicity In Listeria monocytogenes, Pathogenesis and Host Response ed. Goldfine, H. and Shen, H. pp. 81-110. New York: Springer.
17. Ramadurai, L. and Jayaswal, R.K. (1997) Molecular cloning, sequencing, and expression of lytM a unique autolytic gene of Staphylococcus aureus. J Bacteriol 179, 3625-3631.
18. Rawlings, N.D., Morton, F.R. and Barrett, A.J. (2006) MEROPS, the peptidase database. Nucleic Acids Res 34, D270-D272.
19. Recsei, P.A., Gruss, A.D. and Novick, R.P. (1987) Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans. Proc Natl Acad Sci 84, 1127-1131.
20. Sahl, H.G., Hahn, C. and Brandis, H. (1985) Interaction of the staphylococcin-like peptide pep-5 with cell-walls and isolated cell-wall components of Gram-positive bacteria. Zentralbl Bakteriol Mikrobiol Hyg A 260, 197-205.
21. Schindler, C. and Schuhardt, V. (1964) Lysostaphin, a new bacteriolytic agent for the Staphylococcus. Proc Natl Acad Sci 51, 414.
22. Schleifer, K. and Kandler, O. (1972) Peptidoglycan types of bacterial cell-walls and their taxonomic implications. Bacteriol Rev 36, 407-477.
23. Simmonds, R.S., Pearson, L., Kennedy, R.C. and Tagg, J.R. (1996) Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881. Appl Environ Microbiol 62, 4536-4541.
24. Simmonds, R.S., Simpson, W.J. and Tagg, J.R. (1997) Cloning and sequence analysis of zooA, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin. Gene 189, 255-261.
25. Strominger, J.L. and Ghuysen, J.M. (1967) Mechanisms of enzymatic bacteriolysis. Science 156, 213-221.
26. Sugai, M., Fujiwara, T., Akiyama, T., Ohara, M., Komatsuzawa, H., Inoue, S. and Suginaka, H. (1997) Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1. J Bacteriol 179, 1193-1202.
27. Vollmer, W., Blanot, D. and de Pedro, M.A. (2008) Peptidoglycan structure and architecture. FEMS Microbiol Rev 32, 149-167.
28. Yanagida, F., Chen, Y., Onda, T. and Shinohara, T. (2005) Durancin L28-1A, a new bacteriocin from Enterococcus durans L28-1, isolated from soil. Lett Appl Microbiol 40, 430-435.