ArticleJournal of bacteriology2002
An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
- Natural and synthetic antimicrobial peptides against anaerobic bacteria: A review of activities and mechanisms of action.Probiotics and antimicrobial proteins · 2026Review
- Diversity and Functional Roles of the Gut Microbiota in Lepidopteran Insects.Microorganisms · 2022Review
- Insights into the tracking of the cysteine proteinase B COOH-terminal polypeptide of Leishmania (Leishmania) amazonensis by surface plasmon resonance.Parasitology research · 2019Article
- Propionibacterium spp.-source of propionic acid, vitamin B12, and other metabolites important for the industry.Applied microbiology and biotechnology · 2018Review
- Antimicrobial Protein Candidates from the Thermophilic Geobacillus sp. Strain ZGt-1: Production, Proteomics, and Bioinformatics Analysis.International journal of molecular sciences · 2016Article
- The fsr Quorum-Sensing System and Cognate Gelatinase Orchestrate the Expression and Processing of Proprotein EF_1097 into the Mature Antimicrobial Peptide Enterocin O16.Journal of bacteriology · 2015Article
- Isolation, biochemical characterization, and cloning of a bacteriocin from the poultry-associated Staphylococcus aureus strain CH-91.Applied microbiology and biotechnology · 2013Article
- Bacteriocin production, antibiotic susceptibility and prevalence of haemolytic and gelatinase activity in faecal lactic acid bacteria isolated from healthy Ethiopian infants.Microbial ecology · 2013Article
- Multifaceted attributes of dairy propionibacteria: a review.World journal of microbiology & biotechnology · 2012Review
- Specific degradation of the mucus adhesion-promoting protein (MapA) of Lactobacillus reuteri to an antimicrobial peptide.Applied and environmental microbiology · 2010Article
- Milk protein fragments induce the biosynthesis of macedocin, the lantibiotic produced by Streptococcus macedonicus ACA-DC 198.Applied and environmental microbiology · 2010Article
- Glycerol enhances the antifungal activity of dairy propionibacteria.International journal of microbiology · 2010Article
- Identification of the propionicin F bacteriocin immunity gene (pcfI) and development of a food-grade cloning system for Propionibacterium freudenreichii.Applied and environmental microbiology · 2007Article
- Heterologous production of antimicrobial peptides in Propionibacterium freudenreichii.Applied and environmental microbiology · 2005Article
- Proline conformation-dependent antimicrobial activity of a proline-rich histone h1 N-terminal Peptide fragment isolated from the skin mucus of Atlantic salmon.Antimicrobial agents and chemotherapy · 2005Article
- Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii.Applied and environmental microbiology · 2004Article
- Characterization of Bacillus probiotics available for human use.Applied and environmental microbiology · 2004Article
- Prevalence of the genes encoding propionicin T1 and protease-activated antimicrobial peptide and their expression in classical propionibacteria.Applied and environmental microbiology · 2004Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protease-activated antimicrobial peptide (PAMP) and its inactive precursor were purified from the culture supernatant of Propionibacterium jensenii LMG 3032 and characterized at the molecular level. PAMP is a 64-amino-acid cationic peptide of 6,383 Da with physicochemical features similar to those of bacteriocins from gram-positive bacteria. This peptide displayed bactericidal activity against several propionibacteria and lactobacilli. DNA sequencing indicated that the PAMP-encoding gene (pamA) is translated as a proprotein of 198 amino acids with an N-terminal signal peptide of 27 amino acids and that PAMP constitutes the C-terminal part of this precursor. The amino acid sequence of pro-PAMP showed no similarity to those of other known proteins. By using activity tests and mass spectrometry, we showed that PAMP was formed upon protease treatment of the precursor protein. The propionibacteria produced the PAMP precursor constitutively during growth up to a level of approximately 4 mg/liter, but the producing bacteria were unable to activate the precursor. The requirement for an external protease represents a novel strategy for generating antimicrobial peptides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.