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Applied and Environmental Microbiology, December 1998, p. 5057-5060, Vol. 64, No. 12
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Bactericidal Activity of Pediocin PA-1 Is Specifically Inhibited by a 15-mer Fragment That Spans the Bacteriocin from the Center toward the C Terminus

Gunnar Fimland,1,* Ralph Jack,2,3 Günther Jung,2 Ingolf F. Nes,4 and Jon Nissen-Meyer1

Department of Biochemistry, University of Oslo, Oslo,1 and Laboratory of Microbial Gene Technology, Agricultural University of Norway, Ås,4 Norway, and Institut für Organische Chemie, Eberhard-Karls-Universität,2 and ECHAZ Microcollections,3 Tübingen, Germany

Received 25 June 1998/Accepted 10 September 1998

A 15-mer peptide fragment derived from pediocin PA-1 (from residue 20 to residue 34) specifically inhibited the bactericidal activity of pediocin PA-1. The fragment did not inhibit the pediocin-like bacteriocins sakacin P, leucocin A, and curvacin A to nearly the same extent as it inhibited pediocin PA-1. Enterocin A, however, was also significantly inhibited by this fragment, although not as greatly as pediocin PA-1. This is consistent with the fact that enterocin A contains the longest continuous sequence identical to that of pediocin PA-1 in the region spanned by the fragment. The fragment inhibited pediocin PA-1 to a much greater extent than did the other 29 possible 15-mer fragments that span pediocin PA-1. The results suggest that the fragment---by interacting with the target cells and/or pediocin PA-1---interferes specifically with pediocin-target cell interaction.

* Corresponding author. Mailing address: Department of Biochemistry, University of Oslo, Post Box 1041, Blindern, 0316 Oslo, Norway. Phone: 47-22 85 66 32, 47-22 85 66 33, or 47-22 85 73 51. Fax: 47-22 85 44 43. E-mail: jon.nissen-meyer{at}biokjemi.uio.no.

Applied and Environmental Microbiology, December 1998, p. 5057-5060, Vol. 64, No. 12
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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