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Applied and Environmental Microbiology, May 2004, p. 2906-2911, Vol. 70, No. 5
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.5.2906-2911.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Structural and Functional Differences in Two Cyclic Bacteriocins with the Same Sequences Produced by Lactobacilli

Yasushi Kawai,1* Yasuyuki Ishii,1 Kensuke Arakawa,1 Koichiro Uemura,1 Boku Saitoh,1 Junko Nishimura,1 Haruki Kitazawa,1 Yukiko Yamazaki,2 Yoshio Tateno,2 Takatoshi Itoh,3 and Tadao Saito1

Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University, Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555,1 National Institute of Genetics, Mishima 411-8540,2 Laboratory of Animal Food Science, College of Bioresource Science, Nihon University, Fujisawa 252-8510, Japan3

Received 2 June 2003/ Accepted 1 February 2004

Lactobacillus gasseri LA39 and L. reuteri LA6 isolated from feces of the same human infant were found to produce similar cyclic bacteriocins (named gassericin A and reutericin 6, respectively) that cannot be distinguished by molecular weights or primary amino acid sequences. However, reutericin 6 has a narrower spectrum than gassericin A. In this study, gassericin A inhibited the growth of L. reuteri LA6, but reutericin 6 did not inhibit the growth of L. gasseri LA39. Both bacteriocins caused potassium ion efflux from indicator cells and liposomes, but the amounts of efflux and patterns of action were different. Although circular dichroism spectra of purified bacteriocins revealed that both antibacterial peptides are composed mainly of {alpha}-helices, the spectra of the bacteriocins did not coincide. The results of D- and L-amino acid composition analysis showed that two residues and one residue of D-Ala were detected among 18 Ala residues of gassericin A and reutericin 6, respectively. These findings suggest that the different D-alanine contents of the bacteriocins may cause the differences in modes of action, amounts of potassium ion efflux, and secondary structures. This is the first report that characteristics of native bacteriocins produced by wild lactobacillus strains having the same structural genes are influenced by a difference in D-amino acid contents in the molecules.

* Corresponding author. Mailing address: Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University, Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan. Phone: 81 (22) 717-8713. Fax: 81 (22) 717-8715. E-mail: ykawai{at}bios.tohoku.ac.jp.

Applied and Environmental Microbiology, May 2004, p. 2906-2911, Vol. 70, No. 5
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.5.2906-2911.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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