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Applied and Environmental Microbiology, April 2004, p. 2240-2244, Vol. 70, No. 4
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.4.2240-2244.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Prevalence of the Genes Encoding Propionicin T1 and Protease-Activated Antimicrobial Peptide and Their Expression in Classical Propionibacteria

Therese Faye,1* Dag Anders Brede,1 Thor Langsrud,1 Ingolf F. Nes,1 and Helge Holo1,2

Department of Chemistry, Biotechnology and Food Science, Agricultural University of Norway, N-1432 Ås,1 Norwegian Dairies Association, Oslo, Norway2

Received 19 December 2003/ Accepted 22 December 2003

The purpose of this study was to investigate the frequency of production of the bacteriocin propionicin T1 and the protease-activated antimicrobial peptide (PAMP) and their corresponding genes in 64 isolates of classical propionibacteria. This study revealed that these genes are widespread in Propionibacterium jensenii and Propionibacterium thoenii but absent from the remaining species of classical propionibacteria that were studied. The pro-PAMP-encoding gene (pamA) was found in 63% of the P. jensenii strains and 61% of the P. thoenii strains, and all of these strains displayed PAMP activity. The propionicin T1-encoding gene (pctA) was present in 89% of the P. thoenii strains and 54% of the P. jensenii strains. All P. thoenii strains containing the pctA gene exhibited antimicrobial activity corresponding to propionicin T1 activity, whereas only 38% of the pctA-containing P. jensenii strains displayed this activity. Sequencing of the pctA genes revealed the existence of two allelic variants that differed in a single nucleotide in six strains of P. jensenii; in these strains the glycine at position 55 of propionicin T1 was replaced by an aspartate residue (A variant). No strains harboring the A variant showed any antimicrobial activity against propionicin T1-sensitive bacteria. An open reading frame (orf2) located immediately downstream from the pctA gene was absent in three strains containing the G variant of propionicin T1. Two of these strains showed low antimicrobial activity, while the third strain showed no antimicrobial activity at all. The protein encoded by orf2 showed strong homology to ABC transporters, and it has been proposed previously that this protein is involved in the producer immunity against propionicin T1. The limited antimicrobial activity exhibited by the strains lacking orf2 further suggests that this putative ABC transporter plays an important role in propionicin T1 activity.

* Corresponding author. Mailing address: Department of Chemistry, Biotechnology and Food Science, Agricultural University of Norway, P.O. Box 5003, N-1432 Ås, Norway. Phone: 47 64 94 85 33. Fax: 47 64 94 77 20. E-mail: therese.faye{at}ikbm.nlh.no.

Applied and Environmental Microbiology, April 2004, p. 2240-2244, Vol. 70, No. 4
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.4.2240-2244.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Brede, D. A., Faye, T., Stierli, M. P., Dasen, G., Theiler, A., Nes, I. F., Meile, L., Holo, H. (2005). Heterologous Production of Antimicrobial Peptides in Propionibacterium freudenreichii. Appl. Environ. Microbiol. 71: 8077-8084 [Abstract] [Full Text]  
  • Brede, D. A., Faye, T., Johnsborg, O., Odegard, I., Nes, I. F., Holo, H. (2004). Molecular and Genetic Characterization of Propionicin F, a Bacteriocin from Propionibacterium freudenreichii. Appl. Environ. Microbiol. 70: 7303-7310 [Abstract] [Full Text]  


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