Academic Journal
Structure of Lacticaseicin 30 and Its Engineered Variants Revealed an Interplay between the N-Terminal and C-Terminal Regions in the Activity against Gram-Negative Bacteria ; La structure de la lacticaseicine 30 et ses variants ingénieries révèle l'interaction entre les deux extrémités impliquée dans l'activité contre les bactéries Gram-négative.
| العنوان: | Structure of Lacticaseicin 30 and Its Engineered Variants Revealed an Interplay between the N-Terminal and C-Terminal Regions in the Activity against Gram-Negative Bacteria ; La structure de la lacticaseicine 30 et ses variants ingénieries révèle l'interaction entre les deux extrémités impliquée dans l'activité contre les bactéries Gram-négative. |
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| المؤلفون: | Madi-Moussa, Désiré, Deracinois, Barbara, Teiar, Radja, Li, Yanyan, Mihasan, Marius, Flahaut, Christophe, Rebuffat, Sylvie, Coucheney, Françoise, Drider, Djamel |
| المساهمون: | Institut Charles Viollette (ICV) - ULR 7394 (ICV), Université d'Artois (UA)-Université du Littoral Côte d'Opale (ULCO)-Institut Supérieur d'Agriculture-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), BioEcoAgro - Equipe 7 - Health benefit of protein hydrolysates and agro-food co-products: control of production, characterization and valorisation, BioEcoAgro - UMR transfrontalière INRAe - UMRT1158, Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL)-Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL), Molécules de Communication et Adaptation des Micro-organismes (MCAM), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), BioEcoAgro - Equipe 8 - Food and Digestive Microbial Ecosystems: Interactions - Dynamics - Application(s) |
| المصدر: | ISSN: 1999-4923 ; Pharmaceutics ; https://hal.science/hal-03876126 ; Pharmaceutics, 2022, 14 (9), pp.1921. ⟨10.3390/pharmaceutics14091921⟩. |
| بيانات النشر: | CCSD MDPI |
| سنة النشر: | 2022 |
| مصطلحات موضوعية: | Escherichia coli, antimicrobial activity, structure-activity relationship, helical conformation, [SDV]Life Sciences [q-bio] |
| الوصف: | International audience ; Lacticaseicin 30 is one of the five bacteriocins produced by the Gram-positive Lacticaseibacillus paracasei CNCM I-5369. This 111 amino acid bacteriocin is noteworthy for being active against Gram-negative bacilli including Escherichia coli strains resistant to colistin. Prediction of the lacticaseicin 30 structure using the Alphafold2 pipeline revealed a largely helical structure including five helix segments, which was confirmed by circular dichroism. To identify the structural requirements of the lacticaseicin 30 activity directed against Gram-negative bacilli, a series of variants, either shortened or containing point mutations, was heterologously produced in Escherichia coli and assayed for their antibacterial activity against a panel of target strains including Gram-negative bacteria and the Gram-positive Listeria innocua. Lacticaseicin 30 variants comprising either the N-terminal region (amino acids 1 to 39) or the central and C-terminal regions (amino acids 40 to 111) were prepared. Furthermore, mutations were introduced by site-directed mutagenesis to obtain ten bacteriocin variants E6G, T7P, E32G, T33P, T52P, D57G, A74P, Y78S, Y93S and A97P. Compared to lacticaseicin 30, the anti-Gram-negative activity of the N-terminal peptide and variants E32G, T33P and D57G remained almost unchanged, while that of the C-terminal peptide and variants E6G, T7P, T52P, A74P, Y78S, Y93S and A97P was significantly altered. Finally, the N-terminal region was further shortened to keep only the first 20 amino acid part that was predicted to include the first helix. The anti-Gram-negative activity of this truncated peptide was completely abolished. Overall, this study shows that activity of lacticaseicin 30, one of the rare Gram-positive bacteriocins inhibiting Gram-negative bacteria, requires at least two helices in the N-terminal region and that the C-terminal region carries amino acids playing a role in modulation of the activity. Taken together, these data will help to design forthcoming variants ... |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| ردمك: | 978-0-00-856709-5 0-00-856709-3 |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/36145669; PUBMED: 36145669; WOS: 000856709300001 |
| DOI: | 10.3390/pharmaceutics14091921 |
| الاتاحة: | https://hal.science/hal-03876126 https://hal.science/hal-03876126v1/document https://hal.science/hal-03876126v1/file/pharmaceutics-14-01921-v2.pdf https://doi.org/10.3390/pharmaceutics14091921 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.9E2BD9C9 |
| قاعدة البيانات: | BASE |
| ردمك: | 9780008567095 0008567093 |
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| DOI: | 10.3390/pharmaceutics14091921 |