Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity
Enterocin DD14 (EntDD14) is a two-peptide leaderless bacteriocin produced by the <i>Enterococcus faecalis</i> 14 strain previously isolated from meconium. This bacteriocin is mainly active against Gram-positive bacteria. Leaderless bacteriocins do not undergo post-translational modificat...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-01-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/24/2/1517 |
| _version_ | 1797441225641426944 |
|---|---|
| author | Adrián Pérez-Ramos Rabia Ladjouzi Marius Mihasan Radja Teiar Abdellah Benachour Djamel Drider |
| author_facet | Adrián Pérez-Ramos Rabia Ladjouzi Marius Mihasan Radja Teiar Abdellah Benachour Djamel Drider |
| author_sort | Adrián Pérez-Ramos |
| collection | DOAJ |
| description | Enterocin DD14 (EntDD14) is a two-peptide leaderless bacteriocin produced by the <i>Enterococcus faecalis</i> 14 strain previously isolated from meconium. This bacteriocin is mainly active against Gram-positive bacteria. Leaderless bacteriocins do not undergo post-translational modifications and are therefore immediately active after their synthesis. As a result, the cells that produce such bacteriocins have developed means of protection against them which often involve transport systems. In this and our previous work, we constructed different mutants deleted in the genes involved in the transport functions, thus covering all the supposed components of this transport system, using <i>Listeria innocua</i> ATCC 33090 as the indicator strain to assess the activity of externalized EntDD14. We also assessed the self-resistance of the WT and all its engineered derivative mutants against EntDD14, provided extracellularly, in order to evaluate their self-resistance. The results obtained highlight that the ABC transporter constituted by the DdG, H, I, and J proteins contributes to EntDD14 export as well as resistance to an external supply of EntDD14. Our results also have established the essential role of the DdE and DdF proteins as primary transporters dedicated to the externalization of EntDD14. Moreover, the in silico data showed that DdE and DdF appear to assemble in a formation that forms an essential channel for the exit of EntDD14. This channel DdEF may interact with the ABC transporter DdGHIJ in order to control the flow of bacteriocin across the membrane, although the nature of this interaction remains to be elucidated. |
| first_indexed | 2024-03-09T12:19:57Z |
| format | Article |
| id | doaj.art-887630b6a1744fac832aa8895fa8ae5b |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T12:19:57Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-887630b6a1744fac832aa8895fa8ae5b2023-11-30T22:41:40ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-01-01242151710.3390/ijms24021517Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory ActivityAdrián Pérez-Ramos0Rabia Ladjouzi1Marius Mihasan2Radja Teiar3Abdellah Benachour4Djamel Drider5ICV-Institut Charles Viollette, UMR Transfrontalière BioEcoAgro 1158, University Lille, INRAE, University Liège, UPJV, YNCREA, University Artois, University Littoral Côte d’Opale, 59000 Lille, FranceICV-Institut Charles Viollette, UMR Transfrontalière BioEcoAgro 1158, University Lille, INRAE, University Liège, UPJV, YNCREA, University Artois, University Littoral Côte d’Opale, 59000 Lille, FranceBiochemistry and Molecular Biology Laboratory, Faculty of Biology, Alexandru Ioan Cuza University of Iasi, Carol I Blvd, no. 20A, 700506 Iasi, RomaniaICV-Institut Charles Viollette, UMR Transfrontalière BioEcoAgro 1158, University Lille, INRAE, University Liège, UPJV, YNCREA, University Artois, University Littoral Côte d’Opale, 59000 Lille, FranceU2RM-Stress and Virulence, UNICAEN, Esplanade de la Paix, 14000 Caen, FranceICV-Institut Charles Viollette, UMR Transfrontalière BioEcoAgro 1158, University Lille, INRAE, University Liège, UPJV, YNCREA, University Artois, University Littoral Côte d’Opale, 59000 Lille, FranceEnterocin DD14 (EntDD14) is a two-peptide leaderless bacteriocin produced by the <i>Enterococcus faecalis</i> 14 strain previously isolated from meconium. This bacteriocin is mainly active against Gram-positive bacteria. Leaderless bacteriocins do not undergo post-translational modifications and are therefore immediately active after their synthesis. As a result, the cells that produce such bacteriocins have developed means of protection against them which often involve transport systems. In this and our previous work, we constructed different mutants deleted in the genes involved in the transport functions, thus covering all the supposed components of this transport system, using <i>Listeria innocua</i> ATCC 33090 as the indicator strain to assess the activity of externalized EntDD14. We also assessed the self-resistance of the WT and all its engineered derivative mutants against EntDD14, provided extracellularly, in order to evaluate their self-resistance. The results obtained highlight that the ABC transporter constituted by the DdG, H, I, and J proteins contributes to EntDD14 export as well as resistance to an external supply of EntDD14. Our results also have established the essential role of the DdE and DdF proteins as primary transporters dedicated to the externalization of EntDD14. Moreover, the in silico data showed that DdE and DdF appear to assemble in a formation that forms an essential channel for the exit of EntDD14. This channel DdEF may interact with the ABC transporter DdGHIJ in order to control the flow of bacteriocin across the membrane, although the nature of this interaction remains to be elucidated.https://www.mdpi.com/1422-0067/24/2/1517enterocin DD14 (EntDD14)ABC transportersresistance to bacteriocins |
| spellingShingle | Adrián Pérez-Ramos Rabia Ladjouzi Marius Mihasan Radja Teiar Abdellah Benachour Djamel Drider Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity International Journal of Molecular Sciences enterocin DD14 (EntDD14) ABC transporters resistance to bacteriocins |
| title | Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity |
| title_full | Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity |
| title_fullStr | Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity |
| title_full_unstemmed | Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity |
| title_short | Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity |
| title_sort | advances in characterizing the transport systems of and resistance to entdd14 a leaderless two peptide bacteriocin with potent inhibitory activity |
| topic | enterocin DD14 (EntDD14) ABC transporters resistance to bacteriocins |
| url | https://www.mdpi.com/1422-0067/24/2/1517 |
| work_keys_str_mv | AT adrianperezramos advancesincharacterizingthetransportsystemsofandresistancetoentdd14aleaderlesstwopeptidebacteriocinwithpotentinhibitoryactivity AT rabialadjouzi advancesincharacterizingthetransportsystemsofandresistancetoentdd14aleaderlesstwopeptidebacteriocinwithpotentinhibitoryactivity AT mariusmihasan advancesincharacterizingthetransportsystemsofandresistancetoentdd14aleaderlesstwopeptidebacteriocinwithpotentinhibitoryactivity AT radjateiar advancesincharacterizingthetransportsystemsofandresistancetoentdd14aleaderlesstwopeptidebacteriocinwithpotentinhibitoryactivity AT abdellahbenachour advancesincharacterizingthetransportsystemsofandresistancetoentdd14aleaderlesstwopeptidebacteriocinwithpotentinhibitoryactivity AT djameldrider advancesincharacterizingthetransportsystemsofandresistancetoentdd14aleaderlesstwopeptidebacteriocinwithpotentinhibitoryactivity |