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.
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.
Fimland
G
G
Department of Biochemistry, University of Oslo, Oslo, Norway.
Jack
R
R
Jung
G
G
Nes
I F
IF
Nissen-Meyer
J
J
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology*; D001430:Bacteriocins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D008969:Molecular Sequence Data; D000070017:Pediocins; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D000070017:Pediocins; D010446:Peptide Fragments; C071456:sakacin A; C074288:pediocin PA-1; C087217:sakacin P protein, Lactobacillus