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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
 |
ABSTRACT |
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-1interferes specifically with pediocin-target cell interaction.
| |
TEXT |
Bacteria produce ribosomally
synthesized antimicrobial polypeptides, termed bacteriocins.
Bacteriocins produced by gram-positive bacteria are often
membrane-permeabilizing cationic peptides with less than 50 amino acid
residues (1, 18, 21, 23, 25, 31). These peptide bacteriocins
may roughly be classified into two main groups. Group I consists of
bacteriocins, often termed lantibiotics, that contain lanthionine and
or lanthionine-related residues, whereas group II consists of
bacteriocins that lack modified residues. The pediocin-like
bacteriocins constitute a large subgroup within group II
(23): they are all unmodified, they have similar primary
structures, and they exert their bactericidal activity by
permeabilizing the target cell membrane (6, 7).
The first pediocin-like bacteriocins to be characterized were pediocin
PA-1 (14, 19, 22), sakacin P (27, 29), leucocin A
(11), curvacin A (2, 15, 27, 28), and
mesentericin Y105 (13), all produced by lactic acid
bacteria. More recently identified pediocin-like bacteriocins are
carnobacteriocin BM1 and B2 (26), enterocin A (3)
and P (8), bavaricin MN (17), piscicolin 126 (16), piscicocin V1a (4), and bacteriocin 31 (30). All of these bacteriocins exhibit 40 to 60% sequence similarity. The similarity is especially pronounced in the hydrophilic N-terminal half of the peptides. In contrast to the N-terminal half,
the C-terminal half is hydrophobic and/or amphiphilic (9, 10). Thus, it is the C-terminal half of the pediocin-like
bacteriocins which may interact with the hydrophobic part of the target
cell membrane, thereby causing membrane leakage. The recent
three-dimensional nuclear magnetic resonance structural analysis of the
pediocin-like bacteriocin leucocin A shows that upon exposure to
dodecylphosphocholine micelles, the hydrophilic N-terminal half forms a
three-stranded antiparallel 
-sheet and the C-terminal half forms an
amphiphilic 
-helix (10).
Despite similar primary structures, the pediocin-like bacteriocins
differ in their target cell specificity (i.e., they differ in their
antimicrobial spectra) (9). This difference in target cell
specificity, combined with the extensive similarity in amino acid
sequence, makes the pediocin-like bacteriocins well suited for
analyzing the relationship between target cell specificity and primary
structure. Such an analysis may eventually enable the identification of
peptide-cell interactions that are general and of prime importance for
determining whether or not a cell is sensitive to an antimicrobial peptide.
By determining the target cell specificity of hybrid bacteriocins
containing N- and C-terminal regions from different pediocin-like bacteriocins, it has been shown that the C-terminal half of these bacteriocins is an important determinant of target cell specificity (9). Thus, the C-terminal half must interact in a specific manner with an entity on the target cell membrane, an entity which might perhaps also be recognized by peptide fragments derived from the
C-terminal half. In this study, we have identified a 15-mer peptide
fragment derived from the C-terminal half of the pediocin-like
bacteriocin, pediocin PA-1, which inhibits the bactericidal activity of
pediocin PA-1, but not the activity of other closely related
pediocin-like bacteriocins. The results indicate that this fragment
spans a region in the pediocin-like bacteriocins which is important for
target cell specificity. Thus, a target cell specificity-determining
region has been more closely localized within the C-terminal half of
these bacteriocins.
Peptide fragments, bacteriocins, and bacteriocin assay.
Thirty
peptide fragments derived from the sequence of pediocin PA-1 (Fig.
1) were synthesized by standard methods
of solid-phase multiple peptide synthesis with an F-moc strategy. The
peptides were 15 amino acids in length, with an overlap of 14 residues. Thus, the first peptide (fragment 1) spans amino acid residues 1 to 15 of pediocin PA-1, the second (fragment 2) spans residues 2 to 16, and
so on to fragment 30, which starts with residue 30 and ends with
residue 44the last residue in pediocin PA-1. All fragments were
synthesized as acetylated peptide-amides to avoid the effects of
terminal functional groups, and an acetylating capping step was
employed after each synthesis cycle in order to reduce the chances of
"failure sequences" containing internal deletions. Cysteine
residues in pediocin PA-1 were substituted for with -aminobutyric
acid in order to avoid the formation of disulfide linkages between
fragments (and between fragments and bacteriocins) that contain
cysteine residues. All peptides were characterized by electrospray
ionization mass spectrometry (Perkin-Elmer Sciez API III) and
high-performance liquid chromatography; the purities of the final
products were >70%. The synthesized peptides were solubilized to a
concentration of 1 to 10 mg/ml in 0.1% (vol/vol) trifluoroacetic acid
and 10 to 30% (vol/vol) 2-propanol.
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FIG. 1.
Amino acid sequences of pediocin PA-1 (19),
enterocin A (3), curvacin A (2, 28), sakacin P
(29), and leucocin A (11). The regions where the
sequences are identical to the sequence in pediocin PA-1 are boxed.
Regions where the sequences are identical to the sequence of fragment
20 are in black.
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|
Pediocin PA-1, sakacin P, curvacin A, and enterocin A were purified to
homogeneity from 0.5-liter cultures of the producer strain by ammonium
sulfate precipitation and cation exchange, hydrophobic interaction, and
reverse-phase chromatography, essentially as previously described
(3, 22). Enterocin A was produced by Enterococcus
faecium CTC492 (3), whereas the producing strains for
the other bacteriocins were as described in references
22 and 27. Leucocin A was
synthesized and purified to 80 to 90% purity as described in reference
9.
Bacteriocin activity was measured with a microtiter plate assay system
(
24). A 200-µl volume of culture medium, bacteriocin
fractions at twofold dilutions, various amounts of peptide fragments
derived from pediocin PA-1, and the indicator strain
(
Lactobacillus sake NCDO 2714 [type strain] at an optical
density at 610 nm of
0.01) were added to each well of a microtiter
plate. The microtiter
plate cultures were incubated for 10 to 15 h
at 30°C, after which
growth of the indicator strain was measured
spectrophotometrically
at 610 nm with a microtiterplate reader. When
this assay system
is standardized with respect to the amount of
indicator cells
used and the incubation time and temperature,
determination of
bacteriocin activity is reproducible to within a
twofold dilution.
The MIC was defined as the bacteriocin concentration
that inhibited
the growth of the indicator strain by 50% (50% of the
turbidity
of the control culture without bacteriocin). The indicator
strain
and the bacteriocin-producing strains were all grown at 30°C
in
MRS broth
(Oxoid).
A fragment that spans pediocin PA-1 from residue 20 to residue 34 specifically inhibits bacteriocin activity.
The peptide fragments
derived from pediocin PA-1 were all assayed for bacteriocin activity
and for their ability to inhibit the activity of pediocin-like
bacteriocins. None of the fragments showed any bacteriocin activity
when tested at concentrations of 100 µM (data not shown). However,
when tested for their ability to inhibit bacteriocin activity, the
fragment which spans residues 20 to 34 of pediocin PA-1 (fragment 20)
clearly inhibited the bacteriocin activity of pediocin PA-1 (Fig.
2). Adjacent fragments (fragments 18, 19, 21, and 22) also inhibited the bacteriocin activity of pediocin PA-1,
but to a much lesser extent than fragment 20. The other fragments did
not significantly inhibit the bacteriocin activity (Fig. 2).
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FIG. 2.
Inhibition of the bactericidal activities of
pediocin-like bacteriocins due to the presence of 5 µM peptide
fragments derived from pediocin PA-1. Inhibition of the bactericidal
activities is quantitated as the increase in MIC due to the presence of
a fragment. The increase in MIC is defined as the MIC obtained in the
presence of a fragment divided by the MIC obtained in the absence of a
fragment. The MICs were between 0.5 and 0.05 nM for all of the
bacteriocins in the absence of a fragment, with sakacin P having the
highest MIC, enterocin A the lowest, and curvacin A, pediocin PA-1, and
leucocin A having MICs between those of sakacin P and enterocin A.
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|
Fragment 20, and its adjacent fragments, inhibited the bacteriocin
activity of pediocin PA-1 in a specific manner, in the
sense that these
fragments inhibited sakacin P, leucocin A, and
curvacin A to a much
lesser extent than pediocin PA-1 (Fig.
2 and
3). Enterocin A, however, was also
significantly inhibited
by fragment 20, although not as greatly as
pediocin PA-1 (Fig.
3). Interestingly, in the region spanned by
fragment 20, enterocin
A contains the longest continuous sequence that
is identical to
that of pediocin PA-1 (Fig.
1). Moreover, there is a
cysteine
residue in this region in both pediocin PA-1 and enterocin A,
but not in the other three bacteriocins, and this enables the
formation
of a C-terminally-located disulfide bond unique to pediocin
PA-1 and
enterocin A (Fig.
1). The fact that fragment 20 inhibited
pediocin PA-1
to a much greater extent than other bacteriocins
suggests that
inhibition by fragment 20 is not merely due to nonspecific
hydrophobic
interactions between fragment 20 and pediocin-like
bacteriocins in
general. It rather suggests that fragment 20 (by
interacting with the
target cells and or pediocin PA-1) somehow
interferes specifically with
pediocin-target cell interaction.
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FIG. 3.
Inhibition (measured as increase in MIC [see the legend
to Fig. 2]) of the bactericidal activities of pediocin-like
bacteriocins as a function of increasing amounts of fragment 20. The
y axis in the inset has a logarithmic scale, whereas the
y axis in the main figure is linear.
|
|
The primary and three-dimensional structures of these bacteriocins
suggest that their polypeptide chains may be divided into
two
functional domains: the relatively well-conserved hydrophilic
N-terminal
-sheet domain and the somewhat more diverse hydrophobic
or amphiphilic C-terminal
-helical domain (
9,
10). The
well-conserved
N-terminal
-sheet domain must have an important
function common
to the pediocin-like bacteriocin, perhaps to mediate
the initial
unspecific binding of the bacteriocins to target cells
through
electrostatic interactions (
5). The C-terminal
domain, due
to its hydrophobic or amphiphilic character, must be the
domain
which interacts with the hydrophobic part of the membrane. This
is consistent with the observation that chimeric pediocin PA-1,
which
has maltose-binding protein fused to its N terminus, displayed
bactericidal activity, suggesting that the N-terminal part of
the
bacteriocin does not enter the target cell membrane (
20).
Earlier studies using hybrid bacteriocins indicate that the C-terminal
domain is an important determinant of target cell specificity
(
9). The present results suggest that residues in pediocin
that are important for determining target cell specificity are
present
in the region spanned by fragment
20.
A specificity-determining region must interact in a specific manner
with an entity on the target cell membrane. This entity
might simply be
a cell surface binding site, with increased binding
to the cell surface
resulting in higher concentrations of bacteriocins
in the vicinity of
the membrane, which in turn leads to increased
membrane
permeabilization and cytotoxicity. Alternatively, the
entity might be a
membrane component which interacts with residues
in the
specificity-determining region and thereby makes the membrane
more
susceptible to permeabilization. The interaction may be nonchiral,
for
instance, between membrane lipids and side chains of bacteriocin
residues, since strict target cell specificity does not per se
prove
that the antagonistic activity depends on a stereo-specific
interaction. Short membrane-permeabilizing amphiphilic
-helical
bacteriocin-like peptides display strain-specific
antagonistic
activities, which clearly do not depend on stereo-specific
interactions
(
12). Work which is now in progress to identify
residues that
are particularly important for specificity indicates that
residues
within the region spanned by fragment 20 are of importance for
the target cell specificity of pediocin PA-1 and sakacin P
(
9a).
| |
ACKNOWLEDGMENTS |
This work was supported by a Norwegian Research Council grant and
the Deutsche Forschungsgemeinschaft (DFG), Sonderforschungsbereich (SFB) 323.
We thank Linda Bross for expert technical assistance.
| |
FOOTNOTES |
*
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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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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