Pediocin PA-1, a Wide-Spectrum Bacteriocin from Lactic Acid Bacteria

Rodríguez, Juan M.; Martínez, M.; Kok, Jan

doi:10.1080/10408690290825475

Cited by 242 publications

(171 citation statements)

References 156 publications

(196 reference statements)

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“…Attempts were made to induce the phage to lyse the bacteria by incubation with mitomycin C as described in the work of Caldwell et al (1), but all attempts failed (data not shown). There were no open reading frames encoding pediocins, a well-described family of bacteriocins frequently observed in pediococci (5).…”

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Draft Genome Sequence of Probiotic Strain Pediococcus acidilactici MA18/5M

Barreau¹,

Tompkins

Carvalho

2012

J Bacteriol

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Draft Genome Sequence of Probiotic Strain Pediococcus acidilactici MA18/5M

Barreau¹,

Tompkins

Carvalho

2012

J Bacteriol

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“…Bacteriocins are thought to have promise for use as safe food preservatives (7). For example, nisin is currently used in more than 40 countries as an antimicrobial additive (41), and pediocin PA-1 is currently being investigated in this context, as it has a strong inhibitory effect on the food-borne pathogen Listeria monocytogenes (2,38). Pediocin PA-1, composed of 44 residues, is secreted by Pediococcus acidilactici (23,29).…”

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Determination of Essential and Variable Residues in Pediocin PA-1 by NNK Scanning

Tominaga

Hatakeyama

2006

Appl Environ Microbiol

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Pediocin PA-1 is an antimicrobial peptide (called bacteriocin) that shows inhibitory activity against the foodborne pathogen Listeria monocytogenes. To elucidate which residue(s) is responsible for this function, the antimicrobial activities of pediocin PA-1 mutants were evaluated and compared. Each of the 44 native codons was replaced with the NNK triplet oligonucleotide in a technique termed NNK scanning, and 35 mutations at each position were examined for antimicrobial activities using a modified colony overlay screening method. As a consequence, the functional responsibility of each residue was estimated by counting the number of active mutants, allowing us to identify candidate essential/variable residues. Activity was abrogated by many of the mutations at residues Y2, G6, C9, C14, C24, W33, G37, and C44, indicating that these residues may be essential. In contrast, activity was retained by almost all versions harboring mutations at K1, T8, G10, S13, G19, N28, and N41, indicating that these are functionally redundant residues. Sequence analysis revealed that only the wild type was active and 14 and 11 substitutions were inactive at G6 and C14, respectively, while 12 and 11 substitutions were active and 2 and 0 substitutions were inactive at T8 and K1, respectively. These findings suggest that NNK scanning is effective for determining essential and variable residues in pediocin PA-1, leading to an elucidation of structure-function relationships and to improvements in the antimicrobial function efficiently by peptide engineering.Various antimicrobial peptides, called bacteriocins, are produced by lactic acid bacteria to kill or inhibit the growth of closely related species (1). Bacteriocins are thought to have promise for use as safe food preservatives (7). For example, nisin is currently used in more than 40 countries as an antimicrobial additive (41), and pediocin PA-1 is currently being investigated in this context, as it has a strong inhibitory effect on the food-borne pathogen Listeria monocytogenes (2, 38). Pediocin PA-1, composed of 44 residues, is secreted by Pediococcus acidilactici (23,29). More than 20 members of the pediocin-like (class IIa) bacteriocins have been identified to date (16). These peptides contain a consensus YGNGV motif and can be structurally divided into a highly conserved hydrophilic N-terminal domain and a relatively variable hydrophobic C-terminal domain (14). Nuclear magnetic resonance structure (18,42,44) and circular dichroism spectral (17,27,45) analyses have suggested that the N-terminal domain has a threestranded ␤-sheet structure, while the C-terminal domain is folded into an amphiphilic ␣-helical structure. It is thought that the bacteriocins bind to bacteria via electrostatic interactions (4, 28) and then insert into the bacterial membrane via their amphiphilic ␣-helical region, subsequently forming a membrane pore that triggers dissipation of the membrane electrochemical potential (3) and/or nutrient leakage from within the bacterial cell (5,22). A mannose phosphotran...

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“…Also, the dedicated secretion systems (10) associated with bacteriocins produced by lactic acid bacteria have been exploited (19). In this case leader peptides serve as recognition signals for the corresponding ABC transporters and are cleaved during export at a specific processing site adjacent to two conserved glycine residues located at positions Ϫ1 and Ϫ2 (11).…”

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confidence: 99%