ArticleApplied and environmental microbiology2006
Determination of essential and variable residues in pediocin PA-1 by NNK scanning.
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Engineered antimicrobial-derived peptides to manipulate mixed microbial systems.Microbiology spectrum · 2026Article
- Engineered antimicrobial-derived peptides to manipulate mixed microbial systems.bioRxiv : the preprint server for biology · 2025Article
- Molecular Dynamic Study on the Structure and Thermal Stability of Mutant Pediocin PA-1 Peptides Engineered with Cysteine Substitutions.Probiotics and antimicrobial proteins · 2025Article
- Antimicrobial Activity and Immunomodulatory Properties of Acidocin A, the Pediocin-like Bacteriocin with the Non-Canonical Structure.Membranes · 2022Article
- Review
- Mining and Statistical Modeling of Natural and Variant Class IIa Bacteriocins Elucidate Activity and Selectivity Profiles across Species.Applied and environmental microbiology · 2020Article
- Multispecies activity screening of microcin J25 mutants yields antimicrobials with increased specificity toward pathogenic Salmonella species relative to human commensal Escherichia coli.Biotechnology and bioengineering · 2018Article
- Enterocin A mutants identified by saturation mutagenesis enhance potency towards vancomycin-resistant Enterococci.Biotechnology and bioengineering · 2016Article
- Purification and mass spectrometry based characterization of a pediocin produced by Pediococcus acidilactici 13.Molecular biology reports · 2014Article
- Article
- Class IIa bacteriocins: diversity and new developments.International journal of molecular sciences · 2012Review
- Development of Class IIa Bacteriocins as Therapeutic Agents.International journal of microbiology · 2012Article
- Structural and pharmacological effects of ring-closing metathesis in peptides.Molecules (Basel, Switzerland) · 2010Review
- Synthesis of trypsin-resistant variants of the Listeria-active bacteriocin salivaricin P.Applied and environmental microbiology · 2010Article
- Insights into structure-activity relationships in the C-terminal region of divercin V41, a class IIa bacteriocin with high-level antilisterial activity.Applied and environmental microbiology · 2009Article
- Development of innovative pediocin PA-1 by DNA shuffling among class IIa bacteriocins.Applied and environmental microbiology · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pediocin PA-1 is an antimicrobial peptide (called bacteriocin) that shows inhibitory activity against the food-borne 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.
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