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Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity
This review attempts to analyze the mechanism of action and immunity of class IIa bacteriocins. These peptides are promising alternative food preservatives and they have a great potential application in medical sciences. Class IIa bacteriocins act on the cytoplasmic membrane of Gram-positive cells d...
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Published in: | Current genetics 2018-04, Vol.64 (2), p.345-351 |
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description | This review attempts to analyze the mechanism of action and immunity of class IIa bacteriocins. These peptides are promising alternative food preservatives and they have a great potential application in medical sciences. Class IIa bacteriocins act on the cytoplasmic membrane of Gram-positive cells dissipating the transmembrane electrical potential by forming pores. However, their toxicity and immunity mechanism remains elusive. Here we discuss the role of the mannose phosphotransferase system (man-PTS) as the receptor for class IIa bacteriocins and the influence of the membrane composition on the activity of these antimicrobial peptides. A model that is consistent with experimental results obtained by different researchers involves the non-specific binding of the bacteriocin to the negatively charged membrane of target bacteria. This step would facilitate a specific binding to the receptor protein, altering its functionality and forming an independent pore in which the bacteriocin is inserted in the membrane. An immunity protein could specifically recognize and block the pore. Bacteriocins function in bacterial ecosystems and energetic costs associated with their production are also discussed. Theoretical models based on solid experimental evidence are vital to understand bacteriocins mechanism of action and to promote new technological developments. |
doi_str_mv | 10.1007/s00294-017-0757-9 |
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These peptides are promising alternative food preservatives and they have a great potential application in medical sciences. Class IIa bacteriocins act on the cytoplasmic membrane of Gram-positive cells dissipating the transmembrane electrical potential by forming pores. However, their toxicity and immunity mechanism remains elusive. Here we discuss the role of the mannose phosphotransferase system (man-PTS) as the receptor for class IIa bacteriocins and the influence of the membrane composition on the activity of these antimicrobial peptides. A model that is consistent with experimental results obtained by different researchers involves the non-specific binding of the bacteriocin to the negatively charged membrane of target bacteria. This step would facilitate a specific binding to the receptor protein, altering its functionality and forming an independent pore in which the bacteriocin is inserted in the membrane. An immunity protein could specifically recognize and block the pore. Bacteriocins function in bacterial ecosystems and energetic costs associated with their production are also discussed. 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All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-53192eb4a13bd5f78734372efdfecb428dbe1abf0591faa77009d7e6a9d660de3</citedby><cites>FETCH-LOGICAL-c372t-53192eb4a13bd5f78734372efdfecb428dbe1abf0591faa77009d7e6a9d660de3</cites><orcidid>0000-0002-7215-862X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28983718$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ríos Colombo, Natalia S.</creatorcontrib><creatorcontrib>Chalón, Miriam C.</creatorcontrib><creatorcontrib>Navarro, Silvia A.</creatorcontrib><creatorcontrib>Bellomio, Augusto</creatorcontrib><title>Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><addtitle>Curr Genet</addtitle><description>This review attempts to analyze the mechanism of action and immunity of class IIa bacteriocins. 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subjects | Antimicrobial peptides Bacteriocins Binding Biochemistry Biomedical and Life Sciences Cell Biology Forming Immunity Life Sciences Mannose Membrane composition Membrane proteins Membranes Microbial Genetics and Genomics Microbiology Pediocin Peptides Phosphotransferase Plant Sciences Preservatives Proteomics Review Toxicity |
title | Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity |
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