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Applied and Environmental Microbiology, May 2003, p. 2975-2984, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2975-2984.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Enterolysin A, a Cell Wall-Degrading Bacteriocin from Enterococcus faecalis LMG 2333

Trine Nilsen,* Ingolf F. Nes, and Helge Holo

Laboratory of Microbial Gene Technology, Agricultural University of Norway, N-1432 Ås, Norway

Received 15 July 2002/ Accepted 7 February 2003

A novel antimicrobial protein, designated enterolysin A, was purified from an Enterococcus faecalis LMG 2333 culture. Enterolysin A inhibits growth of selected enterococci, pediococci, lactococci, and lactobacilli. Antimicrobial activity was initially detected only on solid media, but by growing the bacteria in a fermentor under optimized production conditions (MRS broth with 4% [wt/vol] glucose, pH 6.5, and a temperature between 25 and 35°C), the bacteriocin activity was increased to 5,120 bacteriocin units ml-1. Enterolysin A production was regulated by pH, and activity was first detected in the transition between the logarithmic and stationary growth phases. Killing of sensitive bacteria by enterolysin A showed a dose-response behavior, and the bacteriocin has a bacteriolytic mode of action. Enterolysin A was purified, and the primary structure was determined by combined amino acid and DNA sequencing. This bacteriocin is translated as a 343-amino-acid preprotein with an sec-dependent signal peptide of 27 amino acids, which is followed by a sequence corresponding to the N-terminal part of the purified protein. Mature enterolysin A consists of 316 amino acids and has a calculated molecular weight of 34,501, and the theoretical pI is 9.24. The N terminus of enterolysin A is homologous to the catalytic domains of different cell wall-degrading proteins with modular structures. These include lysostaphin, ALE-1, zoocin A, and LytM, which are all endopeptidases belonging to the M37 protease family. The N-terminal part of enterolysin A is linked by a threonine-proline-rich region to a putative C-terminal recognition domain, which shows significant sequence identity to two bacteriophage lysins.

* Corresponding author. Present address: Massachusetts General Hospital, Infectious Disease Division, Bacterial Pathogenesis, 65 Landsdowne St., Cambridge, MA 01239. Phone: (617) 768-8741. Fax: (617) 768-8738. E-mail: tnilsen{at}partners.org.

Applied and Environmental Microbiology, May 2003, p. 2975-2984, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2975-2984.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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