This Article Full Text Full Text (PDF) Supplemental material 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 Martin-Visscher, L. A. Articles by Vederas, J. C. Search for Related Content PubMed PubMed Citation Articles by Martin-Visscher, L. A. Articles by Vederas, J. C. Agricola Articles by Martin-Visscher, L. A. Articles by Vederas, J. C.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, August 2008, p. 4756-4763, Vol. 74, No. 15
0099-2240/08/$08.00+0     doi:10.1128/AEM.00817-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Isolation and Characterization of Carnocyclin A, a Novel Circular Bacteriocin Produced by Carnobacterium maltaromaticum UAL307 ^,

Leah A. Martin-Visscher,¹ Marco J. van Belkum,¹ Sylvie Garneau-Tsodikova,^1, Randy M. Whittal,¹ Jing Zheng,¹ Lynn M. McMullen,² and John C. Vederas^1*

Department of Chemistry,¹ Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada²

Received 9 April 2008/ Accepted 9 June 2008

Carnobacterium maltaromaticum UAL307, isolated from fresh pork, exhibits potent activity against a number of gram-positive organisms, including numerous Listeria species. Three bacteriocins were isolated from culture supernatant, and using matrix-assisted laser desorption ionization-time of flight mass spectrometry and Edman sequencing, two of these bacteriocins were identified as piscicolin 126 and carnobacteriocin BM1, both of which have previously been described. The remaining bacteriocin, with a molecular mass of 5,862 Da, could not be sequenced by traditional methods, suggesting that the peptide was either cyclic or N-terminally blocked. This bacteriocin showed remarkable stability over a wide temperature and pH range and was unaffected by a variety of proteases. After digestion with trypsin and -chymotrypsin, the peptide was de novo sequenced by tandem mass spectrometry and a linear sequence deduced, consisting of 60 amino acids. Based on this sequence, the molecular mass was predicted to be 5,880 Da, 18 units higher than the observed molecular mass, which suggested that the peptide has a cyclic structure. Identification of the genetic sequence revealed that this peptide is circular, formed by a covalent linkage between the N and C termini following cleavage of a 4-residue peptide leader sequence. The results of structural studies suggest that the peptide is highly structured in aqueous conditions. This bacteriocin, named carnocyclin A, is the first reported example of a circular bacteriocin produced by Carnobacterium spp.

---

* Corresponding author. Mailing address: Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada. Phone: (780) 492-5475. Fax: (780) 492-2134. E-mail: john.vederas{at}ualberta.ca

Published ahead of print on 13 June 2008.

Supplemental material for this article may be found at http://aem.asm.org/.

Present address: Department of Medicinal Chemistry, Life Sciences Institute, University of Michigan, Ann Arbor, MI.

---

Applied and Environmental Microbiology, August 2008, p. 4756-4763, Vol. 74, No. 15
0099-2240/08/$08.00+0     doi:10.1128/AEM.00817-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Martin-Visscher, L. A., Gong, X., Duszyk, M., Vederas, J. C. (2009). The Three-dimensional Structure of Carnocyclin A Reveals That Many Circular Bacteriocins Share a Common Structural Motif. J. Biol. Chem. 284: 28674-28681 [Abstract] [Full Text]  
• Ito, Y., Kawai, Y., Arakawa, K., Honme, Y., Sasaki, T., Saito, T. (2009). Conjugative Plasmid from Lactobacillus gasseri LA39 That Carries Genes for Production of and Immunity to the Circular Bacteriocin Gassericin A. Appl. Environ. Microbiol. 75: 6340-6351 [Abstract] [Full Text]  
• Liu, X., Han, Y., Yuen, D., Ma, B. (2009). Automated protein (re)sequencing with MS/MS and a homologous database yields almost full coverage and accuracy. Bioinformatics 25: 2174-2180 [Abstract] [Full Text]  
• Kawai, Y., Kusnadi, J., Kemperman, R., Kok, J., Ito, Y., Endo, M., Arakawa, K., Uchida, H., Nishimura, J., Kitazawa, H., Saito, T. (2009). DNA Sequencing and Homologous Expression of a Small Peptide Conferring Immunity to Gassericin A, a Circular Bacteriocin Produced by Lactobacillus gasseri LA39. Appl. Environ. Microbiol. 75: 1324-1330 [Abstract] [Full Text]