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19 results on '"Elise Courvoisier-Dezord"'

1. Synthesis of Second-Generation Analogs of Temporin-SHa Peptide Having Broad-Spectrum Antibacterial and Anticancer Effects

Author

Arif Iftikhar Khan, Shahzad Nazir, Muhammad Nadeem ul Haque, Rukesh Maharjan, Farooq-Ahmad Khan, Hamza Olleik, Elise Courvoisier-Dezord, Marc Maresca, and Farzana Shaheen

Subjects
antimicrobial peptide, temporin SHa, anticancer, Therapeutics. Pharmacology, RM1-950
Abstract

Antimicrobial peptides (AMPs) are a promising class of therapeutic alternatives with broad-spectrum activity against resistant pathogens. Small AMPs like temporin-SHa (1) and its first-generation analog [G10a]-SHa (2) possess notable efficacy against Gram-positive and Gram-negative bacteria. In an effort to further improve this antimicrobial activity, second-generation analogs of 1 were synthesised by replacing the natural glycine residue at position-10 of the parent molecule with atypical amino acids, such as D-Phenylalanine, D-Tyrosine and (2-Naphthyl)-D-alanine, to study the effect of hydrophobicity on antimicrobial efficacy. The resultant analogs (3–6) emerged as broad-spectrum antibacterial agents. Notably, the [G10K]-SHa analog (4), having a lysine substitution, demonstrated a 4-fold increase in activity against Gram-negative (Enterobacter cloacae DSM 30054) and Gram-positive (Enterococcus faecalis DSM 2570) bacteria relative to the parent peptide (1). Among all analogs, [G10f]-SHa peptide (3), featuring a D-Phe substitution, showed the most potent anticancer activity against lung cancer (A549), skin cancer (MNT-1), prostate cancer (PC-3), pancreatic cancer (MiaPaCa-2) and breast cancer (MCF-7) cells, achieving an IC50 value in the range of 3.6–6.8 µM; however, it was also found to be cytotoxic against normal cell lines as compared to [G10K]-SHa (4). Peptide 4 also possessed good anticancer activity but was found to be less cytotoxic against normal cell lines as compared to 1 and 3. These findings underscore the potential of second-generation temporin-SHa analogs, especially analog 4, as promising leads to develop new broad-spectrum antibacterial and anticancer agents.

Published
2024
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2. Design and Synthesis of Novel Amino and Acetamidoaurones with Antimicrobial Activities

Author

Attilio Di Maio, Hamza Olleik, Elise Courvoisier-Dezord, Sophie Guillier, Fabienne Neulat-Ripoll, Romain Haudecoeur, Jean-Michel Bolla, Magali Casanova, Jean-François Cavalier, Stéphane Canaan, Valérie Pique, Yolande Charmasson, Elias Baydoun, Akram Hijazi, Josette Perrier, Marc Maresca, and Maxime Robin

Subjects
aurone, anti-bacterial agents, cytotoxicity tests, structure-activity relationship, Therapeutics. Pharmacology, RM1-950
Abstract

The development of new and effective antimicrobial compounds is urgent due to the emergence of resistant bacteria. Natural plant flavonoids are known to be effective molecules, but their activity and selectivity have to be increased. Based on previous aurone potency, we designed new aurone derivatives bearing acetamido and amino groups at the position 5 of the A ring and managing various monosubstitutions at the B ring. A series of 31 new aurone derivatives were first evaluated for their antimicrobial activity with five derivatives being the most active (compounds 10, 12, 15, 16, and 20). The evaluation of their cytotoxicity on human cells and of their therapeutic index (TI) showed that compounds 10 and 20 had the highest TI. Finally, screening against a large panel of pathogens confirmed that compounds 10 and 20 possess large spectrum antimicrobial activity, including on bioweapon BSL3 strains, with MIC values as low as 0.78 µM. These results demonstrate that 5-acetamidoaurones are far more active and safer compared with 5-aminoaurones, and that benzyloxy and isopropyl substitutions at the B ring are the most promising strategy in the exploration of new antimicrobial aurones.

Published
2024
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4. Design, Synthesis and Characterization of [G10a]-Temporin SHa Dendrimers as Dual Inhibitors of Cancer and Pathogenic Microbes

Author

Arif Iftikhar Khan, Shahzad Nazir, Aaqib Ullah, Muhammad Nadeem ul Haque, Rukesh Maharjan, Shabana U. Simjee, Hamza Olleik, Elise Courvoisier-Dezord, Marc Maresca, and Farzana Shaheen

Subjects
temporin SHa, D-alanine, antimicrobial peptide, Rink amide resin, dendrimer, antibacterial, Microbiology, QR1-502
Abstract

As the technologies for peptide synthesis and development continue to mature, antimicrobial peptides (AMPs) are being widely studied as significant contributors in medicinal chemistry research. Furthermore, the advancement in the synthesis of dendrimers’ design makes dendrimers wonderful nanostructures with distinguishing properties. This study foregrounds a temporin SHa analog, [G10a]-SHa, and its dendrimers as globular macromolecules possessing anticancer and antibacterial activities. These architectures of temporin SHa, named as [G10a]-SHa, its dendrimeric analogs [G10a]2-SHa and [G10a]3-SHa, and [G10a]2-SHa conjugated with a polymer molecule, i.e., Jeff-[G10a]2-SHa, were synthesized, purified on RP-HPLC and UPLC and fully characterized by mass, NMR spectroscopic techniques, circular dichroism, ultraviolet, infrared, dynamic light scattering, and atomic force microscopic studies. In pH- and temperature-dependent studies, all of the peptide dendrimers were found to be stable in the temperature range up to 40–60 °C and pH values in the range of 6–12. Biological-activity studies showed these peptide dendrimers possessed improved antibacterial activity against different strains of both Gram-positive and Gram-negative strains. Together, these dendrimers also possessed potent selective antiproliferative activity against human cancer cells originating from different organs (breast, lung, prostate, pancreas, and liver). The high hemolytic activity of [G10a]2-SHa and [G10a]3-SHa dendrimers, however, limits their use for topical treatment, such as in the case of skin infection. On the contrary, the antibacterial and anticancer activities of Jeff-[G10a]2-SHa, associated with its low hemolytic action, make it potentially suitable for systemic treatment.

Published
2022
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5. The Multifunctional Sactipeptide Ruminococcin C1 Displays Potent Antibacterial Activity In Vivo as Well as Other Beneficial Properties for Human Health

Author

Clarisse Roblin, Steve Chiumento, Cédric Jacqueline, Eric Pinloche, Cendrine Nicoletti, Hamza Olleik, Elise Courvoisier-Dezord, Agnès Amouric, Christian Basset, Louis Dru, Marie Ollivier, Aurélie Bogey-Lambert, Nicolas Vidal, Mohamed Atta, Marc Maresca, Estelle Devillard, Victor Duarte, Josette Perrier, and Mickael Lafond

Subjects
antibiotics, antimicrobial resistance, RiPP, sactipeptide, Ruminococcus gnavus E1, peritonitis infection, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract

The world is on the verge of a major antibiotic crisis as the emergence of resistant bacteria is increasing, and very few novel molecules have been discovered since the 1960s. In this context, scientists have been exploring alternatives to conventional antibiotics, such as ribosomally synthesized and post-translationally modified peptides (RiPPs). Interestingly, the highly potent in vitro antibacterial activity and safety of ruminococcin C1, a recently discovered RiPP belonging to the sactipeptide subclass, has been demonstrated. The present results show that ruminococcin C1 is efficient at curing infection and at protecting challenged mice from Clostridium perfringens with a lower dose than the conventional antibiotic vancomycin. Moreover, antimicrobial peptide (AMP) is also effective against this pathogen in the complex microbial community of the gut environment, with a selective impact on a few bacterial genera, while maintaining a global homeostasis of the microbiome. In addition, ruminococcin C1 exhibits other biological activities that could be beneficial for human health, as well as other fields of applications. Overall, this study, by using an in vivo infection approach, confirms the antimicrobial clinical potential and highlights the multiple functional properties of ruminococcin C1, thus extending its therapeutic interest.

Published
2021
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6. Comparative Structure–Activity Analysis of the Antimicrobial Activity, Cytotoxicity, and Mechanism of Action of the Fungal Cyclohexadepsipeptides Enniatins and Beauvericin

Author

Hamza Olleik, Cendrine Nicoletti, Mickael Lafond, Elise Courvoisier-Dezord, Peiwen Xue, Akram Hijazi, Elias Baydoun, Josette Perrier, and Marc Maresca

Subjects
cyclic fungal peptides, cyclohexadepsipeptide, enniatin, beauvericin, mycotoxin, antibiotic, antimicrobial peptide, AMP, Clostridium perfringens, Medicine
Abstract

Filamentous fungi, although producing noxious molecules such as mycotoxins, have been used to produce numerous drugs active against human diseases such as paclitaxel, statins, and penicillin, saving millions of human lives. Cyclodepsipeptides are fungal molecules with potentially adverse and positive effects. Although these peptides are not novel, comparative studies of their antimicrobial activity, toxicity, and mechanism of action are still to be identified. In this study, the fungal cyclohexadepsipeptides enniatin (ENN) and beauvericin (BEA) were assessed to determine their antimicrobial activity and cytotoxicity against human cells. Results showed that these peptides were active against Gram-positive bacteria, Mycobacterium, and fungi, but not against Gram-negative bacteria. ENN and BEA had a limited hemolytic effect, yet were found to be toxic at low doses to nucleated human cells. Both peptides also interacted with bacterial lipids, causing low to no membrane permeabilization, but induced membrane depolarization and inhibition of macromolecules synthesis. The structure−activity analysis showed that the chemical nature of the side chains present on ENN and BEA (either iso-propyl, sec-butyl, or phenylmethyl) impacts their interaction with lipids, antimicrobial action, and toxicity.

Published
2019
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7. Tight regulation of the intS gene of the KplE1 prophage: a new paradigm for integrase gene regulation.

Author

Gaël Panis, Yohann Duverger, Elise Courvoisier-Dezord, Stéphanie Champ, Emmanuel Talla, and Mireille Ansaldi

Subjects
Genetics, QH426-470
Abstract

Temperate phages have the ability to maintain their genome in their host, a process called lysogeny. For most, passive replication of the phage genome relies on integration into the host's chromosome and becoming a prophage. Prophages remain silent in the absence of stress and replicate passively within their host genome. However, when stressful conditions occur, a prophage excises itself and resumes the viral cycle. Integration and excision of phage genomes are mediated by regulated site-specific recombination catalyzed by tyrosine and serine recombinases. In the KplE1 prophage, site-specific recombination is mediated by the IntS integrase and the TorI recombination directionality factor (RDF). We previously described a sub-family of temperate phages that is characterized by an unusual organization of the recombination module. Consequently, the attL recombination region overlaps with the integrase promoter, and the integrase and RDF genes do not share a common activated promoter upon lytic induction as in the lambda prophage. In this study, we show that the intS gene is tightly regulated by its own product as well as by the TorI RDF protein. In silico analysis revealed that overlap of the attL region with the integrase promoter is widely encountered in prophages present in prokaryotic genomes, suggesting a general occurrence of negatively autoregulated integrase genes. The prediction that these integrase genes are negatively autoregulated was biologically assessed by studying the regulation of several integrase genes from two different Escherichia coli strains. Our results suggest that the majority of tRNA-associated integrase genes in prokaryotic genomes could be autoregulated and that this might be correlated with the recombination efficiency as in KplE1. The consequences of this unprecedented regulation for excessive recombination are discussed.

Published
2010
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8. Laccase-catalyzed functionalization of phenol-modified carbon nanotubes: from grafting of metallopolyphenols to enzyme self-immobilization

Author

Umberto Contaldo, Solène Gentil, Elise Courvoisier-Dezord, Pierre Rousselot-Pailley, Fabrice Thomas, Thierry Tron, Alan Le Goff, Département de Chimie Moléculaire (DCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Solar fuels, hydrogen and catalysis (SolHyCat), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institut des Sciences Moléculaires de Marseille (ISM2), and Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Renewable Energy, Sustainability and the Environment, General Materials Science, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, [CHIM.MATE]Chemical Sciences/Material chemistry
Abstract

International audience; We report the unprecedented use of laccase to functionalize phenol-modified carbon nanotubes (CNTs). Enzymatically-generated metallopolyphenols or the laccase itself can be mildly and efficiently immobilized using the ability of laccase to generate phenoxyl radicals. Electrochemistry, XPS and EPR spectroscopy were used to assess the enzyme-catalyzed CNT functionalization. The efficient immobilization of laccase is confirmed by the high direct bioelectrocatalytic reduction of oxygen with a maximum current density of 1.95 mA cm(-2).

Published
2023

9. Controlled Immobilization of a Palladium Complex/Laccase Hybrid into a Macrocellular Siliceous Host

Author

Fangfang Yang, Pierre Rousselot‐Pailley, Cendrine Nicoletti, A. Jalila Simaan, Bruno Faure, Elise Courvoisier‐Dezord, Agnès Amouric, Yolande Charmasson, Rénal Backov, Thierry Tron, Yasmina Mekmouche, Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Yantai University (YTU), Centre de Recherche Paul Pascal (CRPP), and Université de Bordeaux (UB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[CHIM.ORGA]Chemical Sciences/Organic chemistry, [CHIM.COOR]Chemical Sciences/Coordination chemistry, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis
Abstract

International audience; This study investigates the site-directed immobilization of a hybrid catalyst bearing a biquinoline-based-Pd(II) complex (1) and a robust laccase within cavities of a silica foam to favor veratryl alcohol oxidation. We performed the grafting of 1 at a unique surface located lysine of two laccase variants, either at closed (1⊂UNIK 157) or opposite position (1⊂UNIK 71) of the enzyme oxidation site. After immobilization into the cavities of silica monoliths bearing hierarchical porosity, we show that catalytic activity is dependent on the orientation and loading of each hybrid, 1⊂UNIK 157 being twice as active than 1⊂UNIK 71 (203 TON vs 100 TON) when operating under continuous flow. These systems can be reused 5 times, with an operational activity remaining as high as 40 %. We show that the synergy between 1 and laccase can be tuned within the foam. This work is a proof of concept for controlling the organization of a heterogeneous hybrid catalyst using a Pd/laccase/silica foam.

Published
2023

10. In vitro Applications of the Terpene Mini‐Path 2.0

Author

Julie Couillaud, Agnès Amouric, Elise Courvoisier‐Dezord, Létitia Leydet, Nicolas Schweitzer, Marie‐Noëlle Rosso, Hayat Hage, Margot Loussouarn‐Yvon, Renaud Vincentelli, Jean‐Louis Petit, Véronique de Berardinis, Mireille Attolini, Marc Maresca, Katia Duquesne, Gilles Iacazio, Chalmers University of Technology [Gothenburg, Sweden], Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biodiversité et Biotechnologie Fongiques (BBF), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Génomique métabolique (UMR 8030), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), and J. C. thanks the Ministère de la Recherche for Ph.D. Grant N° 2021AIXM0188/010ED250.

Subjects
[CHIM.ORGA]Chemical Sciences/Organic chemistry, cyclobutyl terpenoid derivatives, [SDV]Life Sciences [q-bio], Organic Chemistry, (+)-δ-cadinol, farnesyl diphosphate, [CHIM.CATA]Chemical Sciences/Catalysis, MESH: Alkyl and Aryl Transferases, Biochemistry, MESH: Terpenes, MESH: Diphosphates, tryprostatin B, MESH: Transferases, terpene mini-path, Molecular Medicine, [CHIM]Chemical Sciences, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology
Abstract

International audience; In 2019 four groups reported independently the development of a simplified enzymatic access to the diphosphates (IPP and DMAPP) of isopentenol and dimethylallyl alcohol (IOH and DMAOH). The former are the two universal precursors of all terpenes. We report here on an improved version of what we call the terpene mini-path as well as its use in enzymatic cascades in combination with various transferases. The goal of this study is to demonstrate the in vitro utility of the TMP in, i) synthesizing various natural terpenes, ii) revealing the product selectivity of an unknown terpene synthase, or iii) generating unnatural cyclobutylated terpenes.

Published
2022

11. Simplified in Vitro and in Vivo Bioaccess to Prenylated Compounds

Author

Jean-Louis Petit, Alyssa Rubini, Véronique de Berardinis, Elise Courvoisier-Dezord, Julie Couillaud, Katia Duquesne, Juan Rico, Gilles Iacazio, Ekaterina Darii, Tarek Hamrouni, Aline Mariage, Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Génomique métabolique (UMR 8030), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), and ANR-14-CE06-0027,Reset,Mini voie de biosynthèse des terpènes(2014)

Subjects
lcsh:Chemistry, Terpene, lcsh:QD1-999, Prenylation, Chemistry, Stereochemistry, In vivo, [SDV]Life Sciences [q-bio], [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], General Chemical Engineering, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, General Chemistry, In vitro
Abstract

All naturally produced terpenes are derived from two universal C5 diphosphate precursors, dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP). Various prenyl transferases use DMAPP ...

Published
2019

12. The Multifunctional Sactipeptide Ruminococcin C1 Displays Potent Antibacterial Activity In Vivo as Well as Other Beneficial Properties for Human Health

Author

Nicolas Vidal, Clarisse Roblin, Mickael Lafond, Louis Dru, Eric Pinloche, Cendrine Nicoletti, Marie Ollivier, Cédric Jacqueline, Mohamed G. Atta, Josette Perrier, Agnès Amouric, Marc Maresca, Steve Chiumento, Christian Basset, Elise Courvoisier-Dezord, Estelle Devillard, Aurélie Bogey-Lambert, Hamza Olleik, Victor Duarte, Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), ADISSEO France SAS, Centre d’Expertise et de Recherche en Nutrition, Biocatalyse (BIOCAT), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Thérapeutiques cliniques et expérimentales des infections (EA 3826) (EA 3826), Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN), BioAzur Biogroup-Vet’Analys Laboratory, Yelen Analytics, Aix-Marseille University ICR, ANR-15-CE21-0020,RUMBA,Caractérisations structurale et fonctionnelle de la Biosynthèse des peptides RumC : une nouvelle famille de bactériocines comme alternative viable aux antibiotiques conventionnels.(2015), ANR-20-CE44-0021,RUMisBAC,Mode d'action et bio-ingénierie des sactipeptides RumC pour vaincre la résistance aux antibiotiques des bactéries à Gram-positif(2020), ANR-10-INBS-0008,ProFI,Infrastructure Française de Protéomique(2010), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), Institut de Chimie Radicalaire (ICR), and Aix Marseille Université (AMU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Antifungal Agents, Clostridium perfringens, Antibiotics, microbiome, antibiotics, lcsh:Chemistry, Bacteriocins, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Ruminococcus gnavus E1, RiPP, lcsh:QH301-705.5, Spectroscopy, Clostridiales, General Medicine, Antimicrobial, 3. Good health, Computer Science Applications, Anti-Bacterial Agents, Vancomycin, Antibacterial activity, medicine.drug, medicine.drug_class, 030106 microbiology, peritonitis infection, Context (language use), Biology, Catalysis, Article, Microbiology, Inorganic Chemistry, 03 medical and health sciences, Antibiotic resistance, [SDV.SP.MED]Life Sciences [q-bio]/Pharmaceutical sciences/Medication, In vivo, medicine, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Microbiome, antimicrobial resistance, Physical and Theoretical Chemistry, Molecular Biology, Organic Chemistry, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, sactipeptide, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, Biofilms, Clostridium Infections, Peptides, Protein Processing, Post-Translational
Abstract

International audience; The world is on the verge of a major antibiotic crisis as the emergence of resistant bacteria is increasing, and very few novel molecules have been discovered since the 1960s. In this context, scientists have been exploring alternatives to conventional antibiotics, such as ribosomally synthesized and post-translationally modified peptides (RiPPs). Interestingly, the highly potent in vitro antibacterial activity and safety of ruminococcin C1, a recently discovered RiPP belonging to the sactipeptide subclass, has been demonstrated. The present results show that ruminococcin C1 is efficient at curing infection and at protecting challenged mice from Clostridium perfringens with a lower dose than the conventional antibiotic vancomycin. Moreover, antimicrobial peptide (AMP) is also effective against this pathogen in the complex microbial community of the gut environment, with a selective impact on a few bacterial genera, while maintaining a global homeostasis of the microbiome. In addition, ruminococcin C1 exhibits other biological activities that could be beneficial for human health, as well as other fields of applications. Overall, this study, by using an in vivo infection approach, confirms the antimicrobial clinical potential and highlights the multiple functional properties of ruminococcin C1, thus extending its therapeutic interest.

Published
2021

13. Tuning of the enzyme ratio in a neutral redox convergent cascade: A key approach for an efficient one‐pot/two‐step biocatalytic whole‐cell system

Author

Véronique de Berardinis, Adrien Debard, Thomas Reignier, Valérie Deyris, Virginie Pellouin, Jean-Louis Petit, Sidiky Ménil, Elise Courvoisier-Dezord, Michelle Sergent, Véronique Alphand, Katia Duquesne, Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Génomique métabolique (UMR 8030), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Institut méditerranéen de biodiversité et d'écologie marine et continentale (IMBE), Avignon Université (AU)-Aix Marseille Université (AMU)-Institut de recherche pour le développement [IRD] : UMR237-Centre National de la Recherche Scientifique (CNRS), Ministère de l'Enseignement Supérieur, de la Recherche et de l'InnovationCost, ANR-10-CD2I-0014,NaturaDyRe,Réactions d'oxydation biocatalysées efficaces pour la synthèse de composés naturels ou énantiopurs(2010), French Ministère de l’Enseignement Supérieur et de la Recherche, Laboratoire d'Instrumentation et Sciences Analytiques (LISA), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), and Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)

Subjects
0106 biological sciences, 0301 basic medicine, Neutral redox system, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV]Life Sciences [q-bio], Baeyer-Villiger Monooxygenase, Cyclohexanol, Bioengineering, Dehydrogenase, 01 natural sciences, Applied Microbiology and Biotechnology, Catalysis, Enzymatic cascade, Mixed Function Oxygenases, Lactones, 03 medical and health sciences, chemistry.chemical_compound, Plasmid, Coumarins, 010608 biotechnology, Escherichia coli, Caproates, Alcohol dehydrogenase, chemistry.chemical_classification, biology, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Escherichia coli Proteins, [CHIM.CATA]Chemical Sciences/Catalysis, Monooxygenase, Combinatorial chemistry, 030104 developmental biology, Enzyme, Metabolic Engineering, chemistry, Biocatalysis, Yield (chemistry), biology.protein, Biotechnology
Abstract

International audience; The efficiency of a versatile in vivo cascade involving a promiscuous alcohol dehydrogenase, obtained from a biodiversity search, and a Baeyer–Villiger monooxygenase was enhanced by the independent control of the production level of each enzyme to produce ε‐caprolactone and 3,4‐dihydrocoumarin. This goal was achieved by adjusting the copy number per cell of Escherichia coli plasmids. We started from the observation that this number generally correlates with the amount of produced enzyme and demonstrated that an in vivo multi‐enzymatic system can be improved by the judicious choice of plasmid, the lower activity of the enzyme that drives the limiting step being counter‐balanced by a higher concentration. Using a preconception‐free approach to the choice of the plasmid type, we observed positive and negative synergetic effects, sometimes unexpected and depending on the enzyme and plasmid combinations. Experimental optimization of the culture conditions allowed us to obtain the complete conversion of cyclohexanol (16 mM) and 1‐indanol (7.5 mM) at a 0.5‐L scale. The yield for the conversion of cyclohexanol was 80% (0.7 g ε‐caprolactone, for the productivity of 244 mg·L −1·h −1) and that for 1‐indanol 60% (0.3 g 3,4‐dihydrocoumarin, for the productivity of 140 mg·L −1·h −1).

Published
2019

14. Production and manipulation of blue copper oxidases for technological applications

Author

Simeng, Zhou, Pierre, Rousselot-Pailley, Lu, Ren, Yolande, Charmasson, Elise Courvoisier, Dezord, Viviane, Robert, Thierry, Tron, and Yasmina, Mekmouche

Subjects
Electron Spin Resonance Spectroscopy, Escherichia coli, Oxidoreductases, Recombinant Proteins
Abstract

Fungal laccases are robust multicopper oxidoreductases. Perfectly amenable to synthetic evolution, the fungal laccase scaffold is a potential generic for the production of tailored biocatalysts, which, in principle, can be secreted at substantial levels in industrially relevant organisms. In this chapter, the strategy we have developed for the rapid production of hundreds of milligram of laccase variants is detailed. It is based on the use of two heterologous expression hosts: the yeast Saccharomyces cerevisiae for a rapid upstream screening and the fungus Aspergillus niger for downstream production. Methods for screening active and nonactive laccase variants, convenient setups for enzyme production in both organisms as well as a methodology for efficient purification of large amounts of recombinant enzymes are given. The general procedure for developing new materials for artificial catalysis is also described.

Published
2018

15. Aurone derivatives as promising antibacterial agents against resistant Gram-positive pathogens

Author

Basile Pérès, Marc Maresca, Hamza Olleik, Akram Hijazi, Josette Perrier, Samir Yahiaoui, Ahcène Boumendjel, Elias Baydoun, Brayan Roulier, Elise Courvoisier-Dezord, Romain Haudecoeur, Josette Raymond, Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Physique et mécanique des milieux hétérogenes (UMR 7636) (PMMH), Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut de Chimie de Strasbourg, Centre National de la Recherche Scientifique (CNRS)-Université Louis Pasteur - Strasbourg I-Institut de Chimie du CNRS (INC), American University of Beirut [Beyrouth] (AUB), Université Paris Descartes - Paris 5 (UPD5), Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Département de pharmacochimie moléculaire (DPM ), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Université Louis Pasteur - Strasbourg I-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), Physique et mécanique des milieux hétérogenes (PMMH), Centre National de la Recherche Scientifique (CNRS)-ESPCI ParisTech-Université Paris Diderot - Paris 7 (UPD7)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), CHU Cochin [AP-HP], Département de pharmacochimie moléculaire (DPM), and Université Grenoble Alpes (UGA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Methicillin-Resistant Staphylococcus aureus, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Selective inhibition, Gram-Positive Bacteria, 01 natural sciences, Microbiology, 03 medical and health sciences, chemistry.chemical_compound, Structure-Activity Relationship, Therapeutic index, Drug Discovery, Aurone, Cytotoxicity, 030304 developmental biology, Gram, Benzofurans, Pharmacology, 0303 health sciences, biology, 010405 organic chemistry, Chemistry, Organic Chemistry, Cell Membrane, General Medicine, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, 3. Good health, 0104 chemical sciences, Anti-Bacterial Agents, Pseudomonas aeruginosa, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Antibacterial activity, Bacteria
Abstract

International audience; A set of variously substituted aurones was synthesized and evaluated against Methicillin-Resistant S. aureus (MRSA) and P. aeruginosa. Several analogues were found active against MRSA, but no effect was recorded against P. aeruginosa. Compounds 27, 30 and 33 showed low cytotoxicity, and were tested against a full range of bacterial (Gram-positive and Gram-negative) and fungal species, including resistant strains. These aurones displayed a selective inhibition of Gram-positive bacteria with excellent Therapeutic Index values, while showing no significant action on several Gram-negative strains, H. pylori and V. alginolyticus being the only susceptible strains among the Gram-negative bacteria tested. A per-meabilization assay showed that the antibacterial activity of at least some of the aurones could be linked to alterations of the bacterial membrane. Overall, this study endorses the use of the aurone scaffold for the development of new potent and selective antibacterial agents.

Published
2018

16. Production and manipulation of blue copper oxidases for technological applications

Author

Yolande Charmasson, Yasmina Mekmouche, Simeng Zhou, Lu Ren, Thierry Tron, Elise Courvoisier Dezord, Viviane Robert, Pierre Rousselot-Pailley, Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)-École Centrale de Marseille (ECM), and Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, chemistry.chemical_classification, Laccase, biology, Aspergillus niger, Saccharomyces cerevisiae, New materials, [CHIM.CATA]Chemical Sciences/Catalysis, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, 010402 general chemistry, biology.organism_classification, 01 natural sciences, Yeast, 0104 chemical sciences, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], 03 medical and health sciences, 030104 developmental biology, Enzyme, Directed mutagenesis, chemistry, Biochemistry, Heterologous expression, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], ComputingMilieux_MISCELLANEOUS
Abstract

Fungal laccases are robust multicopper oxidoreductases. Perfectly amenable to synthetic evolution, the fungal laccase scaffold is a potential generic for the production of tailored biocatalysts, which, in principle, can be secreted at substantial levels in industrially relevant organisms. In this chapter, the strategy we have developed for the rapid production of hundreds of milligram of laccase variants is detailed. It is based on the use of two heterologous expression hosts: the yeast Saccharomyces cerevisiae for a rapid upstream screening and the fungus Aspergillus niger for downstream production. Methods for screening active and nonactive laccase variants, convenient setups for enzyme production in both organisms as well as a methodology for efficient purification of large amounts of recombinant enzymes are given. The general procedure for developing new materials for artificial catalysis is also described.

Published
2018

17. Mechanistic and functional aspects of the Ruminococcin C sactipeptide isoforms

Author

Lama Shamseddine, Clarisse Roblin, Iris Veyrier, Christian Basset, Lisa De Macedo, Anne Boyeldieu, Marc Maresca, Cendrine Nicoletti, Gaël Brasseur, Sylvie Kieffer-Jaquinod, Élise Courvoisier-Dezord, Agnès Amouric, Philippe Carpentier, Nathalie Campo, Mathieu Bergé, Patrice Polard, Josette Perrier, Victor Duarte, and Mickael Lafond

Subjects
Biochemistry, Medical biochemistry, Microbiology, Bacteriology, Science
Abstract

Summary: In a scenario where the discovery of new molecules to fight antibiotic resistance is a public health concern, ribosomally synthesized and post-translationally modified peptides constitute a promising alternative. In this context, the Gram-positive human gut symbiont Ruminococcus gnavus E1 produces five sactipeptides, Ruminococcins C1 to C5 (RumC1–C5), co-expressed with two radical SAM maturases. RumC1 has been shown to be effective against various multidrug resistant Gram-positives clinical isolates. Here, after adapting the biosynthesis protocol to obtain the four mature RumC2-5 we then evaluate their antibacterial activities. Establishing first that both maturases exhibit substrate tolerance, we then observed a variation in the antibacterial efficacy between the five isoforms. We established that all RumCs are safe for humans with interesting multifunctionalities. While no synergies where observed for the five RumCs, we found a synergistic action with conventional antibiotics targeting the cell wall. Finally, we identified crucial residues for antibacterial activity of RumC isoforms.

Published
2023
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18. Tight Regulation of the intS Gene of the KplE1 Prophage: A New Paradigm for Integrase Gene Regulation

Author

Emmanuel Talla, Yohann Duverger, Elise Courvoisier-Dezord, Gaël Panis, Stéphanie Champ, Mireille Ansaldi, Laboratoire de chimie bactérienne (LCB), and Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Gene Expression Regulation, Viral, Cancer Research, lcsh:QH426-470, Prophages, Virus Integration, [SDV]Life Sciences [q-bio], Green Fluorescent Proteins, Molecular Sequence Data, Biology, Microbiology, Genome, Viral Proteins, 03 medical and health sciences, RNA, Transfer, Lysogenic cycle, Escherichia coli, Genetics, Recombinase, Promoter Regions, Genetic, Molecular Biology, Gene, Genetics (clinical), Ecology, Evolution, Behavior and Systematics, Prophage, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Recombination, Genetic, 0303 health sciences, Binding Sites, Microbiology/Microbial Evolution and Genomics, Microbiology/Microbial Growth and Development, Base Sequence, Integrases, Models, Genetic, 030302 biochemistry & molecular biology, Integrase, lcsh:Genetics, Microscopy, Fluorescence, Attachment Sites, Microbiological, Mutation, biology.protein, Research Article
Abstract

Temperate phages have the ability to maintain their genome in their host, a process called lysogeny. For most, passive replication of the phage genome relies on integration into the host's chromosome and becoming a prophage. Prophages remain silent in the absence of stress and replicate passively within their host genome. However, when stressful conditions occur, a prophage excises itself and resumes the viral cycle. Integration and excision of phage genomes are mediated by regulated site-specific recombination catalyzed by tyrosine and serine recombinases. In the KplE1 prophage, site-specific recombination is mediated by the IntS integrase and the TorI recombination directionality factor (RDF). We previously described a sub-family of temperate phages that is characterized by an unusual organization of the recombination module. Consequently, the attL recombination region overlaps with the integrase promoter, and the integrase and RDF genes do not share a common activated promoter upon lytic induction as in the lambda prophage. In this study, we show that the intS gene is tightly regulated by its own product as well as by the TorI RDF protein. In silico analysis revealed that overlap of the attL region with the integrase promoter is widely encountered in prophages present in prokaryotic genomes, suggesting a general occurrence of negatively autoregulated integrase genes. The prediction that these integrase genes are negatively autoregulated was biologically assessed by studying the regulation of several integrase genes from two different Escherichia coli strains. Our results suggest that the majority of tRNA-associated integrase genes in prokaryotic genomes could be autoregulated and that this might be correlated with the recombination efficiency as in KplE1. The consequences of this unprecedented regulation for excisive recombination are discussed., Author Summary Temperate bacteriophages are widespread bacterial viruses that have the ability to replicate passively in their hosts as long as no stressful conditions are encountered, a process called lysogeny. Prophage-encoded genes may benefit the host in several ways such as providing resistance to antibiotics, increased pathogenicity, or increased fitness. Most temperate phages insert their genome into the host's chromosome by site-specific recombination. After prophage induction, usually under stressful conditions, the excisive recombination constitutes a key step toward productive phage development. In this paper, we study the regulation of integrase genes that encode the enzyme required for integrative as well as excisive recombination. We noticed that for prophages inserted in or near tRNA genes the orientation of the integrase gene relative to the tRNA is crucial for its regulation.

Published
2010

19. Recombinant Tyrosinase from Polyporus arcularius : Overproduction in Escherichia coli , Characterization, and Use in a Study of Aurones as Tyrosinase Effectors

Author

Romain Haudecoeur, Ahcène Boumendjel, Petr Man, Alena Křenková, Marius Réglier, Eva Marková, Yasmina Mekmouche, Ludmila Martínková, Renaud Hardré, Michael Kotik, Elise Courvoisier-Dezord, Institute of Microbiology of the Czech Academy of Sciences (MBU / CAS), Czech Academy of Sciences [Prague] (CAS), Department of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, ICT Prague-Technicka 3, Département de pharmacochimie moléculaire (DPM ), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC), REGLIER, Marius, Institute of Microbiology of the Czech Academy of Sciences [Prague, Czech Republic] (MBU / CAS), and Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, 0301 basic medicine, [CHIM.INOR] Chemical Sciences/Inorganic chemistry, Tyrosinase, Gene Expression, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, medicine.disease_cause, 01 natural sciences, Fungal Proteins, 03 medical and health sciences, Enzyme activator, 010608 biotechnology, medicine, Escherichia coli, [CHIM.COOR]Chemical Sciences/Coordination chemistry, ComputingMilieux_MISCELLANEOUS, Polyporus arcularius, Benzofurans, chemistry.chemical_classification, Fungal protein, biology, Effector, Monophenol Monooxygenase, [CHIM.ORGA]Chemical Sciences/Organic chemistry, General Chemistry, [CHIM.COOR] Chemical Sciences/Coordination chemistry, biology.organism_classification, [CHIM.ORGA] Chemical Sciences/Organic chemistry, Polyporus, Recombinant Proteins, Kinetics, 030104 developmental biology, Enzyme, Biochemistry, chemistry, General Agricultural and Biological Sciences
Abstract

Tyrosinases act in the development of organoleptic properties of tea, raisins, etc., but also cause unwanted browning of fruits, vegetables, and mushrooms. The tyrosinase from Agaricus bisporus has been used as a model to study tyrosinase inhibitors, which are also indispensable in the treatment of skin pigmentation disorders. However, this model has disadvantages such as side enzyme activities and the presence of multiple isoenzymes. Therefore, we aimed to introduce a new tyrosinase model. The pro-tyrosinase from Polyporus arcularius was overproduced in Escherichia coli. Trypsin digestion led to a cleavage after R388 and hence enzyme activation. The tyrosinase was a homodimer and transformed L-DOPA and tert-butylcatechol preferentially. Various aurons were examined as effectors of this enzyme. 2'- and 3'-hydroxyaurones acted as its activators and 2',4'-dihydroxyaurone as an inhibitor, whereas 4'-hydroxyaurones were its substrates. The enzyme is a promising model for tyrosinase effector studies, being a single isoenzyme and void of side enzyme activities.

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