Conformational changes of pediocin in an aqueous medium monitored by Fourier transform infrared spectroscopy: a biological implication

Gaussier, Hélène; Lavoie, Marie; Subirade, Muriel

doi:10.1016/s0141-8130(03)00018-7

Cited by 14 publications

(17 citation statements)

References 50 publications

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“…The peptide's tyrosine wave number shifting from 1,515.14 cm Ϫ1 to 1,511.5 cm Ϫ1 is also evidence of the peptide's change to a more hydrophobic environment (9,38). These results support the hypothesis that this peptide could insert into the DPPC bilayer (22). As a consequence, the FTIR spectrum of Lac705␤ in the amide IЈ region reveals an important conformational reorganization upon the interaction with DPPC vesicles (Fig.…”

Section: Discussionsupporting

confidence: 66%

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Molecular View by Fourier Transform Infrared Spectroscopy of the Relationship between Lactocin 705 and Membranes: Speculations on Antimicrobial Mechanism

Castellano

Vignolo

Farı́as

et al. 2007

Appl Environ Microbiol

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Lactocin 705 is a bacteriocin whose activity depends upon the complementation of two peptides, termed Lac705␣ and Lac705␤. Neither Lac705␣ nor Lac705␤ displayed bacteriocin activity by itself when the growth of sensitive cells was monitored. To obtain molecular insights into the lactocin 705 mechanism of action, Fourier transform infrared spectroscopy was used to investigate the interactions of each peptide (Lac705␣ and Lac705␤) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705␣ interacts with the interfacial region inducing dehydration, Lac705␤ peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705␣ and Lac705␤ peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705␣ could induce the dehydration of the bilayer interfacial region, and the Lac705␤ peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization.In the last decade, there has been a growing interest in biopreservation through the use of microorganisms and/or their metabolites to prevent food spoilage and to extend the shelf life of foods (7,34,42). Lactic acid bacteria (LAB) are of particular interest as biopreservative organisms. The preserving effects of these organisms are due to the production of antimicrobial substances, including hydrogen peroxide, organic acid, and bacteriocins (16,36). Bacteriocins are ribosomally synthetized antimicrobial peptides active against closely related bacteria. The major classes of bacteriocins produced by LAB include: lantibiotics, small heat-stable peptides, large heat-labile proteins, and complex proteins. Most of the bacteriocins produced by LAB belong to class II, which can be subdivided into Listeria-active peptides (IIa), two-peptide bacteriocins (IIb), sec-dependent bacteriocins (IIc), and bacteriocins that do not belong to the other subgroups (IId) (27). The potential application of LAB bacteriocins as food preservatives requires an in-depth knowledge of how they exert their bactericidal effects. Many bacteriocins appear to elicit their lethal effects by permeabilizing the cell membrane of target organisms, in certain cases by targeting intermediates of cell wall biosynthesis (10, 44) or possibly proteins of the sugar phosphotransferase systems (24, 39). The meat isolate Lactobacillus curvatus CRL705 (formerly identified as Lactobacillus casei CRL705) produces lactocin 705, a small antimicrobial substance that belongs to the class IIb bacteriocins, whose activities depend upon the complementation of two peptides, termed Lac705␣ (GMSGYIQGIPDFLKGYLHGISAANKHK KGRLGY; pI ϭ 9.87) and Lac705␤ (GFWGGLGYIAGRVG AAYGHAQASANNHHSPING; pI ϭ 8.61) (17, 18). Lactocin 705 exerted an inhibitory effect on the indicator strain Lactobac...

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Section: Discussionsupporting

confidence: 66%

“…However, this wave number is affected by the tyrosine's local environment being different according to whether it is exposed to water or to a hydrophobic environment. For example, it increases upon peptide unfolding (22,38). Therefore, this vibration mode may represent a marker providing information relative to the peptide surroundings (9).…”

Section: Resultsmentioning

confidence: 99%

Molecular View by Fourier Transform Infrared Spectroscopy of the Relationship between Lactocin 705 and Membranes: Speculations on Antimicrobial Mechanism

Castellano

Vignolo

Farı́as

et al. 2007

Appl Environ Microbiol

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“…The data for Listeria innocua death induced by pediocin PA-1 reveal that its activity maximum is reached near pD 6 and decreases at pD 7 and 8 (15,30). A relation between activity and structure alterations has not yet been completely established.…”

mentioning

confidence: 99%

“…A relation between activity and structure alterations has not yet been completely established. The loss of activity as a function of pD seems to be associated to a structural reorganization and a decrease in the protein flexibility that in turn results in an irreversible aggregation upon heating (30). The C-terminal region is first involved in the aggregation process, resulting in a total inactivation of the protein (30).…”

mentioning

confidence: 99%

“…Pediocin can exist in a soluble and hydrophobic structural form (16). In an aqueous environment, pediocin presents an unordered structure as seen by circular dichroism (75) and Fourier transform infrared (FTIR) spectroscopy (30), whereas upon adsorption to vesicles, a structural rearrangement occurs. It was inferred from circular dichroism data that the peptide forms a ␤␣ domain in the presence of phospholipid membrane (75).…”

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confidence: 99%

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Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Gaussier

Lefèvre

Subirade

2003

Appl Environ Microbiol

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To obtain molecular insights into the action mode of antimicrobial activity of pediocin PA-1, the interactions between this bacteriocin and dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylglycerol (DMPG) model membranes have been investigated in D 2 O at pD 6 by Fourier transform infrared spectroscopy. The interactions were monitored with respect to alteration of the secondary structure of pediocin, as registered by the amide I band, and phospholipid conformation, as revealed by the methylene s (CH 2 ) and carbonyl (CAO) stretching vibrations. The results show that no interaction between pediocin and DMPC occurs. By contrast, pediocin undergoes a structural reorganization in the presence of DMPG. Upon heating, pediocin self-aggregates, which is not observed for this pD in aqueous solution. The gel-to-crystalline phase transition of DMPG shifts to higher temperatures with a concomitant dehydration of the interfacial region. Our results indicate that pediocin is an extrinsic peptide and that its action mechanism may lie in a destabilization of the cell membrane.Pediocin PA-1 is a 44-amino-acid (molecular mass, 4,629 Da; pI, 9.6) (35) class IIa bacteriocin (38) produced by Pediococcus acidilactici PAC 1.0 and naturally found in fermented sausages (37) or other meat and vegetable fermentations (5). Its sequence is highly homologous to other class IIa bacteriocins (59). The N-terminal 20-amino-acid half of pediocin is in the majority of cases polar or cationic and highly conserved, with the consensus sequence Y3-G4-N5-G6-V7. The C-terminal half (residues A21 to C44) is much less polar and less conserved, containing a hypothetical hydrophobic membrane interaction domain. Two disulfide bonds stabilize the peptide structure, the one between the residues 24 and 44 accounting for its broad range of antimicrobial activity (17). Because of its specific antimicrobial activity against the foodborne psychrotrophic pathogen Listeria monocytogenes, pediocin PA-1 can potentially serve as a nontoxic food preservative to improve the quality, naturalness, and safety (55) of dairy and meat products.The data for Listeria innocua death induced by pediocin PA-1 reveal that its activity maximum is reached near pD 6 and decreases at pD 7 and 8 (15, 30). A relation between activity and structure alterations has not yet been completely established. The loss of activity as a function of pD seems to be associated to a structural reorganization and a decrease in the protein flexibility that in turn results in an irreversible aggregation upon heating (30). The C-terminal region is first involved in the aggregation process, resulting in a total inactivation of the protein (30). The N-terminal region participates in the aggregation process in a second step. Pediocin can exist in a soluble and hydrophobic structural form (16). In an aqueous environment, pediocin presents an unordered structure as seen by circular dichroism (75) and Fourier transform infrared (FTIR) spectroscopy (30), whereas upon adsorption to vesicles, a structura...

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Isolation and characterization of antifungal peptides produced by Bacillus amyloliquefaciens LBM5006

et al. 2010

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Bacillus amyloliquefaciens LBM 5006 produces antagonistic activity against pathogenic bacteria and phytopathogenic fungi, including Aspergillus spp., Fusarium spp., and Bipolaris sorokiniana. PCR analysis revealed the presence of ituD, but not sfp genes, coding for iturin and surfactin, respectively. The antimicrobial substance produced by this strain was isolated by ammonium sulfate precipitation, gel filtration chromatography and 1-butanol extraction. The ultraviolet spectrum was typical of a polypeptide and the infrared spectrum indicates the presence of peptide bonds and acyl group(s). The antimicrobial substance was resistant to proteolytic enzymes and heat treatment, and was reactive with ninhydrin. Mass spectroscopy analysis indicated that B. amyloliquefaciens LBM 5006 produces two antimicrobial peptides, with main peaks at m/z 1,058 Da and 1,464 Da, corresponding to iturin-like and fengycin-like peptides, respectively. B. amyloliquefaciens LBM 5006 showed significant activity against phytopatogenic fungi, showing potential for use as a biocontrol agent or production of antifungal preparations.

show abstract

Conformational changes of pediocin in an aqueous medium monitored by Fourier transform infrared spectroscopy: a biological implication

Cited by 14 publications

References 50 publications

Molecular View by Fourier Transform Infrared Spectroscopy of the Relationship between Lactocin 705 and Membranes: Speculations on Antimicrobial Mechanism

Molecular View by Fourier Transform Infrared Spectroscopy of the Relationship between Lactocin 705 and Membranes: Speculations on Antimicrobial Mechanism

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Isolation and characterization of antifungal peptides produced by Bacillus amyloliquefaciens LBM5006

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