An Antimicrobial Peptide Is Produced by Extracellular Processing of a Protein from Propionibacterium jensenii
| Autor: | Helge Holo, Therese Faye, Dag Anders Brede, Ingolf F. Nes, Thor Langsrud |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Proteases
medicine.medical_treatment Molecular Sequence Data Antimicrobial peptides Peptide Microbial Sensitivity Tests Biology Microbial Communities and Interactions Microbiology Bacteriocins Bacteriocin medicine Amino Acid Sequence Protein Precursors Molecular Biology chemistry.chemical_classification Protease Base Sequence Lysostaphin Propionibacterium Antimicrobial biology.organism_classification Extracellular Matrix Biochemistry chemistry Endopeptidase K Protein Processing Post-Translational Sequence Analysis Bacteria Antimicrobial Cationic Peptides |
| Zdroj: | Journal of Bacteriology. 184:3649-3656 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.184.13.3649-3656.2002 |
| Popis: | Antimicrobial peptides are produced by all kinds of organisms, from bacteria to mammals. In higher organisms these compounds are produced as an innate host defense mechanism to protect against pathogenic attack, whereas microorganisms presumably use these compounds as weapons in the competition for limited resources. A large number of antimicrobial peptides have been isolated from amphibians (35), fish (2, 22), insects (32), mammals (13), plants (1), and different microorganisms (12). Antimicrobial proteins and peptides from bacteria include toxins like diphtheria and cholera toxins (24, 25), bacteriolytic enzymes like lysostaphin (30) and hemolysins (8), and bacteriocins and bacteriocin-like peptides (10, 12). Numerous bacteriocins have been characterized from gram-positive bacteria, and some of them show a relatively broad spectrum of inhibition. Antimicrobial peptides produced by food-grade organisms such as lactic acid bacteria and propionibacteria have received special interest due to their potential applications in food preservation (33). The classical propionibacteria have a long history of use in dairy fermentations, in particular the production of Swiss-type cheeses. A few antimicrobial peptides from these bacteria have been described so far (7, 9, 14, 15, 17, 21, 29), and only two bacteriocins have been characterized at the molecular level (7, 17). Bacteria use a number of different mechanisms to regulate and produce active peptides and proteins. Most conventional bacteriocins are produced as precursor peptides, which are modified posttranslationally inside the cell or at the cell exterior during export to generate their biologically active forms (12). However, it has been shown that antimicrobial peptides from both bacteria (27, 28) and higher organisms (23, 31) can be produced from the degradation of larger proteins. In this work we describe a novel antimicrobial peptide isolated from Propionibacterium jensenii LMG 3032. This compound is secreted from the cell as an inactive proprotein which is proteolytically activated by proteases in the environment. The mature peptide has several features in common with well-known antimicrobial peptides like class II bacteriocins and antimicrobial cationic peptides from higher organisms. This is to our knowledge the first bacteriocin-like peptide formed from an inactive extracellular protein by an external protease. |
| Databáze: | OpenAIRE |
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