Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19

Atrih, Abdelmadjid; Rekhif, N.; Moir, Arthur J. G.; Lebrihi, Ahmed; Lefèbvre, G.

doi:10.1016/s0168-1605(01)00482-2

Cited by 170 publications

(112 citation statements)

References 30 publications

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“…Consistent with earlier studies (Atrih et al, 2001 ;Bhunia et al, 1991), the binding of the peptides to target cells was reduced upon reducing the electrostatic interactions by increasing the ionic strength by adding NaCl (0n3 M) or MgCl # (50 mM ; results not shown). These salts also inhibited the activity of sakacin P and all the sakacin P variants ; their MIC values increased by between twoand 100-fold, depending on the salt, the salt concentration, the indicator strain and the peptide (results not shown).…”

Section: Figsupporting

confidence: 89%

“…The former mutation reduced the potency by only two-to threefold, whereas the latter reduced it by three-to fivefold (Table M Henderson et al (1992), Marugg et al (1992) ; coagulin, Le Marrec et al (2000) ; sakacin P, Tichaczek et al (1994) ; piscicolin (same as piscicolin V1a), Jack et al (1996), Bhugaloo-Vial et al (1996) ;mundticin, Bennik et al (1998) ;sakacin 5x, Vaughan et al (2001) ; leucocin C, G. Fimland and others (unpublished) ;bacteriocin 31, Tomita et al (1996) ; curvacin A (same as sakacin A), Holck et al (1992), Tichaczek et al (1993) ;carnobacteriocin BM1, Quadri et al (1994) ; enterocin P, Cintas et al (1997) ; enterocin A, Aymerich et al (1996) ; divercin V41, Me! tivier et al (1998) ;carnobacteriocin B2, Quadri et al (1994) ; leucocin A, Hastings et al (1991) ; mesentericin Y105, Fleury et al (1996) ; and plantaricin C19 (not the complete sequence), Atrih et al (2001). Fig.…”

Section: Effect On Activity Of Mutations That Render Sakacin P Less Cmentioning

confidence: 99%

“…Target-cell-binding studies. Binding of sakacin P and sakacin P variants to target cells was measured in a manner similar to that described by Atrih et al (2001) and Bhunia et al (1991). L. sake target cells from a 100 ml overnight culture were pelleted, washed in 50 ml MRS, and finally suspended in 20 ml MRS ; 0n5 ml of this cell suspension was then incubated for 20 min at 20 mC with 0n5 ml culture supernatant containing sakacin P or a mutated variant of sakacin P (about 1 µg ml − ").…”

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Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P

2002

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The significance of charged residues for the target-cell binding, potency and specificity of pediocin-like bacteriocins has been studied by site-directed mutagenesis of sakacin P. Most of the charged residues are located in the N-terminal half, which is thought to mediate the initial binding of these bacteriocins to target cells through electrostatic interaction. All the mutated peptides in which the net positive charge was reduced by one (by replacing a charged residue with threonine) exhibited reduced binding to target cells and a 2-15-fold reduction in potency. The least deleterious of these mutations was the removal of the positive charge in position 8 (H8T). This mutation was, in fact, less deleterious than the conservative His to Lys mutation, indicating that the positive charge in position 8 per se is not of major importance. Somewhat more deleterious was the removal of positive charges at the N-and C-terminal ends (K1T, K43T). Most deleterious was the elimination of the positive charge at positions 11 and (but to a lesser extent) 12, demonstrating the importance of the cationic patch in the middle of the N-terminal half of pediocin-like bacteriocins. Mutated peptides in which the net positive charge was increased by one were also constructed. Some of these exhibited increased cell binding and a potency that was the same as (44K, i.e. an extra positive charge at the Cterminus), or somewhat greater (T20K) than, that of sakacin P, whereas others (0K, i.e. an extra positive charge at the N-terminus) had reduced potency. Sakacin P contains only one negatively charged residue (Asp17). This negative charge and its orientation in space were crucial for activity, since the Asp to Asn mutation and (especially) the conservative Asp to Glu mutation were deleterious. Mutations that made the peptide less cationic had, overall, less effect on the potency toward the Carnobacterium piscicola strain than on the potency toward the three other strains tested, whereas the opposite was the case for mutations that made the peptide more cationic. Thus, charged residues in the N-terminal half may -apparently via the initial electrostatic binding of the bacteriocin to target cells -influence the target-cell specificity.Keywords : antimicrobial peptides, mutagenesis, lactic acid bacteria INTRODUCTIONMany Gram-positive bacteria produce antimicrobial peptides, generally termed bacteriocins. These peptides are usually cationic, less than 50 amino acid residues long, contain an amphiphilic or hydrophobic region, and often kill their target cells by permeabilizing the cell membrane (Nes et al., 1996(Nes et al., , 2002. Antimicrobial peptides with these characteristics are also produced by plants and a wide variety of animals, including humans, and are thus widely distributed in nature M. Kazazic, J. Nissen-Meyer and G. Fimland phospholipid-containing membranes and\or acidic cell walls, whereas their amphiphilic\hydrophobic character enables membrane permeabilization. The pediocin-like bacteriocins constitute a dominant and well-studie...

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Section: Figsupporting

confidence: 89%

Section: Effect On Activity Of Mutations That Render Sakacin P Less Cmentioning

confidence: 99%

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confidence: 99%

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Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P

2002

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“…Both class I and class II plantaricins have been previously identified from different L. plantarum strains (Atrih et al, 2001;Enan et al, 2002;Galvez et al, 2007;Gong et al, 2010;Hata et al, 2010;Hernandez et al, 2005;Holo et al, 2001;Tiwari and Srivastava, 2008;Zhang et al, 2013) and were found to show high antimicrobial activities against L. monocytogenes (Gong et al, 2010;Holo et al, 2001;Tiwari and Srivastava, 2008).…”

Section: Introductionmentioning

confidence: 99%

Purification and Molecular Characterization of Two-Antimicrobial Peptides Produced by Lactobacillus plantarum DU10

Amina¹,

Noureddine²,

Arul³

et al. 2015

International J. of Biological Chemistry

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The aim of this study was the partial characterization of plantaricin MZ, a two-component antimicrobial peptides produced by the putative probiotic bacteria Lactobacillus plantarum DU10, which was isolated from Algerian raw camel milk. This biomolecule was secreted in the supernatant of a L. plantarum DU10 culture and showed diverse spectrum of antimicrobial activities against several pathogenic bacteria. The activity as determined by the proteolytic action of trypsin, pepsin and proteinase K, plantaricin MZ was maintained even after a treatment at 121°C for 15°C and a pH range from 2-10. This putative probiotic strain was found to produce antimicrobial substances proteinaceous in nature. Molecular mass determination was estimated with tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis, then confirmed by mass-assisted laser desorption ionization time of flight mass spectrometry. The producing strain and its antimicrobial peptides may find an application as a bio-preservative agent.

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“…The growth of LAB itself shows positive effects, since LAB produce lactic acid during sugar fermentation, that inhibits the majority of unwanted microorganisms (pathogenic and spoilage) due to the acidification of the environment (Atrih et al, 2001). Moreover, several LAB are able to secrete some metabolites with specific antagonistic activity and antibacterial effects such as antifungal compounds (Lavermicocca et al, 2000), bacteriocins and antibiotics (De Vuyst and Vandamme, 1994;Höltzel et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Extension of Tosèla cheese shelf-life using non-starter lactic acid bacteria

et al. 2011

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a b s t r a c tSix strains of non-starter lactic acid bacteria (NSLAB) were used to extend the shelf-life of the fresh cheese Tosèla manufactured with pasteurised cows' milk. The acidification kinetics of three Lactobacillus paracasei, one Lactobacillus rhamnosus and two Streptococcus macedonicus were studied in synthetic milk medium. Lb. paracasei NdP78 and NdP88 and S. macedonicus NdP1 and PB14-1 showed an interesting acidifying capacity and were further characterised for growth in UHT milk and production of antimicrobial compounds. Lb. paracasei NdP78 and S. macedonicus NdP1 grew more than 2 log cycles in 6 h. Lb. paracasei NdP78 was also found to produce a bacteriocin-like inhibitory substance (BLIS) active against Listeria monocytogenes. The four NSLAB strains (singly or in combination) were used to produce experimental pilotscale cheeses which were compared by a panel. The cheese manufactured with the mixed culture Lb. paracasei NdP78 -S. macedonicus NdP1 was the most appreciated for its sensory properties. The cheeses produced at factory-scale showed higher concentrations of lactobacilli (7.90 log CFU/g) and streptococci (6.10 log CFU/g), but a lower development of coliforms (3.10 log CFU/g) and staphylococci (2.78 log CFU/g) than control cheese (4.86, 4.89, 4.93 and 5.00 log CFU/g of lactobacilli, streptococci, coliforms and staphylococci, respectively) processed without NSLAB addition. The food pathogens Salmonella spp. and Listeria monocytogenes were never detected. The dominance of the species inoculated was demonstrated by denaturing gradient gel electrophoresis (DGGE), whereas strain recognition was evaluated by randomly amplified polymorphic DNA (RAPD)-PCR. From the results obtained, Lb. paracasei NdP78 and S. macedonicus NdP1 were able to persist during the storage of Tosèla cheese and their combination influenced positively the sensory characteristics and shelf-life of the final product.

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Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19

Cited by 170 publications

References 30 publications

Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P

Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P

Purification and Molecular Characterization of Two-Antimicrobial Peptides Produced by Lactobacillus plantarum DU10

Extension of Tosèla cheese shelf-life using non-starter lactic acid bacteria

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