This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cintas, L. M.
Right arrow Articles by Nes, I. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cintas, L. M.
Right arrow Articles by Nes, I. F.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2000, p. 6806-6814, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Biochemical and Genetic Evidence that Enterococcus faecium L50 Produces Enterocins L50A and L50B, the sec-Dependent Enterocin P, and a Novel Bacteriocin Secreted without an N-Terminal Extension Termed Enterocin Q

Luis M. Cintas,1,* Pilar Casaus,1,dagger Carmen Herranz,2 Leiv Sigve Håvarstein,1 Helge Holo,1 Pablo E. Hernández,2 and Ingolf F. Nes1

Laboratory of Microbial Gene Technology, Department of Biotechnological Sciences, Agricultural University of Norway, N-1432 Ås, Norway,1 and Departamento de Nutrición y Bromatología III, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain2

Received 16 June 2000/Accepted 23 September 2000

Enterococcus faecium L50 grown at 16 to 32°C produces enterocin L50 (EntL50), consisting of EntL50A and EntL50B, two unmodified non-pediocin-like peptides synthesized without an N-terminal leader sequence or signal peptide. However, the bacteriocin activity found in the cell-free culture supernatants following growth at higher temperatures (37 to 47°C) is not due to EntL50. A purification procedure including cation-exchange, hydrophobic interaction, and reverse-phase liquid chromatography has shown that the antimicrobial activity is due to two different bacteriocins. Amino acid sequences obtained by Edman degradation and DNA sequencing analyses revealed that one is identical to the sec-dependent pediocin-like enterocin P produced by E. faecium P13 (L. M. Cintas, P. Casaus, L. S. Håvarstein, P. E. Hernández, and I. F. Nes, Appl. Environ. Microbiol. 63:4321-4330, 1997) and the other is a novel unmodified non-pediocin-like bacteriocin termed enterocin Q (EntQ), with a molecular mass of 3,980. DNA sequencing analysis of a 963-bp region of E. faecium L50 containing the enterocin P structural gene (entP) and the putative immunity protein gene (entiP) reveals a genetic organization identical to that previously found in E. faecium P13. DNA sequencing analysis of a 1,448-bp region identified two consecutive but diverging open reading frames (ORFs) of which one, termed entQ, encodes a 34-amino-acid protein whose deduced amino acid sequence was identical to that obtained for EntQ by amino acid sequencing, showing that EntQ, similarly to EntL50A and EntL50B, is synthesized without an N-terminal leader sequence or signal peptide. The second ORF, termed orf2, was located immediately upstream of and in opposite orientation to entQ and encodes a putative immunity protein composed of 221 amino acids. Bacteriocin production by E. faecium L50 showed that EntP and EntQ are produced in the temperature range from 16 to 47°C and maximally detected at 47 and 37 to 47°C, respectively, while EntL50A and EntL50B are maximally synthesized at 16 to 25°C and are not detected at 37°C or above.

* Corresponding author. Present address: Departamento de Nutrición y Bromatología III, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain. Phone: 34-913943751. Fax: 34-913943743. E-mail: lcintas{at}eucmax.sim.ucm.es.

dagger Present address: Centros Comerciales Carrefour, División de Calidad, 28022 Madrid, Spain.

Journal of Bacteriology, December 2000, p. 6806-6814, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Izquierdo, E., Cai, Y., Marchioni, E., Ennahar, S. (2009). Genetic Identification of the Bacteriocins Produced by Enterococcus faecium IT62 and Evidence that Bacteriocin 32 Is Identical to Enterocin IT. Antimicrob. Agents Chemother. 53: 1907-1911 [Abstract] [Full Text]  
  • Basanta, A., Herranz, C., Gutierrez, J., Criado, R., Hernandez, P. E., Cintas, L. M. (2009). Development of Bacteriocinogenic Strains of Saccharomyces cerevisiae Heterologously Expressing and Secreting the Leaderless Enterocin L50 Peptides L50A and L50B from Enterococcus faecium L50. Appl. Environ. Microbiol. 75: 2382-2392 [Abstract] [Full Text]  
  • Izquierdo, E., Bednarczyk, A., Schaeffer, C., Cai, Y., Marchioni, E., Van Dorsselaer, A., Ennahar, S. (2008). Production of Enterocins L50A, L50B, and IT, a New Enterocin, by Enterococcus faecium IT62, a Strain Isolated from Italian Ryegrass in Japan. Antimicrob. Agents Chemother. 52: 1917-1923 [Abstract] [Full Text]  
  • Sanchez, J., Borrero, J., Gomez-Sala, B., Basanta, A., Herranz, C., Cintas, L. M., Hernandez, P. E. (2008). Cloning and Heterologous Production of Hiracin JM79, a Sec-Dependent Bacteriocin Produced by Enterococcus hirae DCH5, in Lactic Acid Bacteria and Pichia pastoris. Appl. Environ. Microbiol. 74: 2471-2479 [Abstract] [Full Text]  
  • Fujita, K., Ichimasa, S., Zendo, T., Koga, S., Yoneyama, F., Nakayama, J., Sonomoto, K. (2007). Structural Analysis and Characterization of Lacticin Q, a Novel Bacteriocin Belonging to a New Family of Unmodified Bacteriocins of Gram-Positive Bacteria. Appl. Environ. Microbiol. 73: 2871-2877 [Abstract] [Full Text]  
  • Srionnual, S., Yanagida, F., Lin, L.-H., Hsiao, K.-N., Chen, Y.-s. (2007). Weissellicin 110, a Newly Discovered Bacteriocin from Weissella cibaria 110, Isolated from Plaa-Som, a Fermented Fish Product from Thailand. Appl. Environ. Microbiol. 73: 2247-2250 [Abstract] [Full Text]  
  • Nes, I. F., Diep, D. B., Holo, H. (2007). Bacteriocin Diversity in Streptococcus and Enterococcus. J. Bacteriol. 189: 1189-1198 [Full Text]  
  • Diep, D. B., Skaugen, M., Salehian, Z., Holo, H., Nes, I. F. (2007). Common mechanisms of target cell recognition and immunity for class II bacteriocins. Proc. Natl. Acad. Sci. USA 104: 2384-2389 [Abstract] [Full Text]  
  • Criado, R., Gutierrez, J., Martin, M., Herranz, C., Hernandez, P. E., Cintas, L. M. (2006). Immunochemical Characterization of Temperature-Regulated Production of Enterocin L50 (EntL50A and EntL50B), Enterocin P, and Enterocin Q by Enterococcus faecium L50. Appl. Environ. Microbiol. 72: 7634-7643 [Abstract] [Full Text]  
  • Criado, R., Diep, D. B., Aakra, A., Gutierrez, J., Nes, I. F., Hernandez, P. E., Cintas, L. M. (2006). Complete Sequence of the Enterocin Q-Encoding Plasmid pCIZ2 from the Multiple Bacteriocin Producer Enterococcus faecium L50 and Genetic Characterization of Enterocin Q Production and Immunity.. Appl. Environ. Microbiol. 72: 6653-6666 [Abstract] [Full Text]  
  • Martin-Platero, A. M., Valdivia, E., Ruiz-Rodriguez, M., Soler, J. J., Martin-Vivaldi, M., Maqueda, M., Martinez-Bueno, M. (2006). Characterization of Antimicrobial Substances Produced by Enterococcus faecalis MRR 10-3, Isolated from the Uropygial Gland of the Hoopoe (Upupa epops).. Appl. Environ. Microbiol. 72: 4245-4249 [Abstract] [Full Text]  
  • Gutierrez, J., Criado, R., Martin, M., Herranz, C., Cintas, L. M., Hernandez, P. E. (2005). Production of Enterocin P, an Antilisterial Pediocin-Like Bacteriocin from Enterococcus faecium P13, in Pichia pastoris. Antimicrob. Agents Chemother. 49: 3004-3008 [Abstract] [Full Text]  
  • Herranz, C., Driessen, A. J. M. (2005). Sec-Mediated Secretion of Bacteriocin Enterocin P by Lactococcus lactis. Appl. Environ. Microbiol. 71: 1959-1963 [Abstract] [Full Text]  
  • Pons, A.-M., Delalande, F., Duarte, M., Benoit, S., Lanneluc, I., Sable, S., Van Dorsselaer, A., Cottenceau, G. (2004). Genetic Analysis and Complete Primary Structure of Microcin L. Antimicrob. Agents Chemother. 48: 505-513 [Abstract] [Full Text]  
  • Vaughan, A., Eijsink, V. G. H., van Sinderen, D. (2003). Functional Characterization of a Composite Bacteriocin Locus from Malt Isolate Lactobacillus sakei 5. Appl. Environ. Microbiol. 69: 7194-7203 [Abstract] [Full Text]  
  • Yamamoto, Y., Togawa, Y., Shimosaka, M., Okazaki, M. (2003). Purification and Characterization of a Novel Bacteriocin Produced by Enterococcus faecalis Strain RJ-11. Appl. Environ. Microbiol. 69: 5746-5753 [Abstract] [Full Text]  
  • Gajic, O., Buist, G., Kojic, M., Topisirovic, L., Kuipers, O. P., Kok, J. (2003). Novel Mechanism of Bacteriocin Secretion and Immunity Carried Out by Lactococcal Multidrug Resistance Proteins. J. Biol. Chem. 278: 34291-34298 [Abstract] [Full Text]  
  • Sanchez-Hidalgo, M., Maqueda, M., Galvez, A., Abriouel, H., Valdivia, E., Martinez-Bueno, M. (2003). The Genes Coding for Enterocin EJ97 Production by Enterococcus faecalis EJ97 Are Located on a Conjugative Plasmid. Appl. Environ. Microbiol. 69: 1633-1641 [Abstract] [Full Text]  
  • Franz, C. M. A. P., Grube, A., Herrmann, A., Abriouel, H., Starke, J., Lombardi, A., Tauscher, B., Holzapfel, W. H. (2002). Biochemical and Genetic Characterization of the Two-Peptide Bacteriocin Enterocin 1071 Produced by Enterococcus faecalis FAIR-E 309. Appl. Environ. Microbiol. 68: 2550-2554 [Abstract] [Full Text]  
  • Cintas, L. M., Casaus, M. P., Herranz, C., Nes, I. F., Hernandez, P. E. (2001). Review: Bacteriocins of Lactic Acid Bacteria. Food Science and Technology International 7: 281-305 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»