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.
Department of Biochemistry,
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.
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