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  1. Article: Editorial for the Special Issue "Microbial Nonribosomal Synthesis of Secondary Metabolites".

    Cociancich, Stéphane / Leclère, Valérie

    Microorganisms

    2022  Volume 10, Issue 5

    Abstract: Microbial secondary metabolites are natural products that display various therapeutical or agrochemical relevant activities (e [ ... ]. ...

    Abstract Microbial secondary metabolites are natural products that display various therapeutical or agrochemical relevant activities (e [...].
    Language English
    Publishing date 2022-05-21
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms10051064
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Nonribosomal Peptide Synthesis Definitely Working Out of the Rules.

    Duban, Matthieu / Cociancich, Stéphane / Leclère, Valérie

    Microorganisms

    2022  Volume 10, Issue 3

    Abstract: Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called ... ...

    Abstract Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called nonribosomal peptide synthetases. These synthetases are organized in modules constituted of adenylation, thiolation, and condensation core domains. As such, each module governs, according to the collinearity rule, the incorporation of a monomer within the growing peptide. The release of the peptide from the assembly chain is finally performed by a terminal core thioesterase domain. Secondary domains with modifying catalytic activities such as epimerization or methylation are sometimes included in the assembly lines as supplementary domains. This assembly line structure is analyzed by bioinformatics tools to predict the sequence and structure of the final peptides according to the sequence of the corresponding synthetases. However, a constantly expanding literature unravels new examples of nonribosomal synthetases exhibiting very rare domains and noncanonical organizations of domains and modules, leading to several amazing strategies developed by microorganisms to synthesize nonribosomal peptides. In this review, through several examples, we aim at highlighting these noncanonical pathways in order for the readers to perceive their complexity.
    Language English
    Publishing date 2022-03-07
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms10030577
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Nonribosomal Peptide Synthesis Definitely Working Out of the Rules

    Duban, Matthieu / Cociancich, Stéphane / Leclère, Valérie

    Microorganisms. 2022 Mar. 07, v. 10, no. 3

    2022  

    Abstract: Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called ... ...

    Abstract Nonribosomal peptides are microbial secondary metabolites exhibiting a tremendous structural diversity and a broad range of biological activities useful in the medical and agro-ecological fields. They are built up by huge multimodular enzymes called nonribosomal peptide synthetases. These synthetases are organized in modules constituted of adenylation, thiolation, and condensation core domains. As such, each module governs, according to the collinearity rule, the incorporation of a monomer within the growing peptide. The release of the peptide from the assembly chain is finally performed by a terminal core thioesterase domain. Secondary domains with modifying catalytic activities such as epimerization or methylation are sometimes included in the assembly lines as supplementary domains. This assembly line structure is analyzed by bioinformatics tools to predict the sequence and structure of the final peptides according to the sequence of the corresponding synthetases. However, a constantly expanding literature unravels new examples of nonribosomal synthetases exhibiting very rare domains and noncanonical organizations of domains and modules, leading to several amazing strategies developed by microorganisms to synthesize nonribosomal peptides. In this review, through several examples, we aim at highlighting these noncanonical pathways in order for the readers to perceive their complexity.
    Keywords agroecology ; bioinformatics ; ligases ; methylation ; nonribosomal peptides
    Language English
    Dates of publication 2022-0307
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms10030577
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  4. Article ; Online: Specificity and genetic polymorphism in the Vfm quorum sensing system of plant pathogenic bacteria of the genus Dickeya.

    Hugouvieux-Cotte-Pattat, Nicole / Royer, Monique / Gueguen, Erwan / Le Guen, Paul / Süssmuth, Roderich D / Reverchon, Sylvie / Cociancich, Stéphane

    Environmental microbiology

    2022  Volume 24, Issue 3, Page(s) 1467–1483

    Abstract: The Vfm quorum sensing (QS) system is preponderant for the virulence of different species of the bacterial genus Dickeya. The vfm gene cluster encodes 26 genes involved in the production, sensing or transduction of the QS signal. To date, the Vfm QS ... ...

    Abstract The Vfm quorum sensing (QS) system is preponderant for the virulence of different species of the bacterial genus Dickeya. The vfm gene cluster encodes 26 genes involved in the production, sensing or transduction of the QS signal. To date, the Vfm QS signal has escaped detection by analytical chemistry methods. However, we report here a strain-specific polymorphism in the biosynthesis genes vfmO and vfmP, which is predicted to be related to the production of different analogues of the QS signal. Consequently, the Vfm communication could be impossible between strains possessing different variants of the genes vfmO/P. We constructed three Vfm QS biosensor strains possessing different vfmO/P variants and compared these biosensors for their responses to samples prepared from 34 Dickeya strains possessing different vfmO/P variants. A pattern of specificity was demonstrated, providing evidence that the polymorphism in the genes vfmO/P determines the biosynthesis of different analogues of the QS signal. Unexpectedly, this vfmO/P-dependent pattern of specificity is linked to a polymorphism in the ABC transporter gene vfmG, suggesting an adaptation of the putative permease VfmG to specifically bind different analogues of the QS signal. Accordingly, we discuss the possible involvement of VfmG as co-sensor of the Vfm two-component regulatory system.
    MeSH term(s) Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Dickeya ; Gene Expression Regulation, Bacterial ; Polymorphism, Genetic ; Quorum Sensing/genetics
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2022-01-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.15889
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Specificity and genetic polymorphism in the Vfm quorum sensing system of plant pathogenic bacteria of the genus Dickeya

    Hugouvieux‐Cotte‐Pattat, Nicole / Royer, Monique / Gueguen, Erwan / Le Guen, Paul / Süssmuth, Roderich D. / Reverchon, Sylvie / Cociancich, Stéphane

    Environmental microbiology. 2022 Mar., v. 24, no. 3

    2022  

    Abstract: The Vfm quorum sensing (QS) system is preponderant for the virulence of different species of the bacterial genus Dickeya. The vfm gene cluster encodes 26 genes involved in the production, sensing or transduction of the QS signal. To date, the Vfm QS ... ...

    Abstract The Vfm quorum sensing (QS) system is preponderant for the virulence of different species of the bacterial genus Dickeya. The vfm gene cluster encodes 26 genes involved in the production, sensing or transduction of the QS signal. To date, the Vfm QS signal has escaped detection by analytical chemistry methods. However, we report here a strain‐specific polymorphism in the biosynthesis genes vfmO and vfmP, which is predicted to be related to the production of different analogues of the QS signal. Consequently, the Vfm communication could be impossible between strains possessing different variants of the genes vfmO/P. We constructed three Vfm QS biosensor strains possessing different vfmO/P variants and compared these biosensors for their responses to samples prepared from 34 Dickeya strains possessing different vfmO/P variants. A pattern of specificity was demonstrated, providing evidence that the polymorphism in the genes vfmO/P determines the biosynthesis of different analogues of the QS signal. Unexpectedly, this vfmO/P‐dependent pattern of specificity is linked to a polymorphism in the ABC transporter gene vfmG, suggesting an adaptation of the putative permease VfmG to specifically bind different analogues of the QS signal. Accordingly, we discuss the possible involvement of VfmG as co‐sensor of the Vfm two‐component regulatory system.
    Keywords ABC transporters ; Dickeya ; analytical chemistry ; biosensors ; biosynthesis ; genetic polymorphism ; multigene family ; virulence
    Language English
    Dates of publication 2022-03
    Size p. 1467-1483.
    Publishing place John Wiley & Sons, Inc.
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.15889
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  6. Article: Draft Genome Sequence of Xanthomonas sacchari Strain LMG 476.

    Pieretti, Isabelle / Bolot, Stéphanie / Carrère, Sébastien / Barbe, Valérie / Cociancich, Stéphane / Rott, Philippe / Royer, Monique

    Genome announcements

    2015  Volume 3, Issue 2

    Abstract: We report the high-quality draft genome sequence of Xanthomonas sacchari strain LMG 476, isolated from sugarcane. The genome comparison of this strain with a previously sequenced X. sacchari strain isolated from a distinct environmental source should ... ...

    Abstract We report the high-quality draft genome sequence of Xanthomonas sacchari strain LMG 476, isolated from sugarcane. The genome comparison of this strain with a previously sequenced X. sacchari strain isolated from a distinct environmental source should provide further insights into the adaptation of this species to different habitats and its evolution.
    Language English
    Publishing date 2015-03-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2704277-7
    ISSN 2169-8287
    ISSN 2169-8287
    DOI 10.1128/genomeA.00146-15
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  7. Article: What makes Xanthomonas albilineans unique amongst xanthomonads?

    Pieretti, Isabelle / Pesic, Alexander / Petras, Daniel / Royer, Monique / Süssmuth, Roderich D / Cociancich, Stéphane

    Frontiers in plant science

    2015  Volume 6, Page(s) 289

    Abstract: Xanthomonas albilineans causes leaf scald, a lethal disease of sugarcane. Compared to other species of Xanthomonas, X. albilineans exhibits distinctive pathogenic mechanisms, ecology and taxonomy. Its genome, which has experienced significant erosion, ... ...

    Abstract Xanthomonas albilineans causes leaf scald, a lethal disease of sugarcane. Compared to other species of Xanthomonas, X. albilineans exhibits distinctive pathogenic mechanisms, ecology and taxonomy. Its genome, which has experienced significant erosion, has unique genomic features. It lacks two loci required for pathogenicity in other plant pathogenic species of Xanthomonas: the xanthan gum biosynthesis and the Hrp-T3SS (hypersensitive response and pathogenicity-type three secretion system) gene clusters. Instead, X. albilineans harbors in its genome an SPI-1 (Salmonella pathogenicity island-1) T3SS gene cluster usually found in animal pathogens. X. albilineans produces a potent DNA gyrase inhibitor called albicidin, which blocks chloroplast differentiation, resulting in the characteristic white foliar stripe symptoms. The antibacterial activity of albicidin also confers on X. albilineans a competitive advantage against rival bacteria during sugarcane colonization. Recent chemical studies have uncovered the unique structure of albicidin and allowed us to partially elucidate its fascinating biosynthesis apparatus, which involves an enigmatic hybrid PKS/NRPS (polyketide synthase/non-ribosomal peptide synthetase) machinery.
    Language English
    Publishing date 2015-04-24
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2613694-6
    ISSN 1664-462X
    ISSN 1664-462X
    DOI 10.3389/fpls.2015.00289
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  8. Article: Full Genome Sequence Analysis of Two Isolates Reveals a Novel Xanthomonas Species Close to the Sugarcane Pathogen Xanthomonas albilineans.

    Pieretti, Isabelle / Cociancich, Stéphane / Bolot, Stéphanie / Carrère, Sébastien / Morisset, Alexandre / Rott, Philippe / Royer, Monique

    Genes

    2015  Volume 6, Issue 3, Page(s) 714–733

    Abstract: Xanthomonas albilineans is the bacterium responsible for leaf scald, a lethal disease of sugarcane. Within the Xanthomonas genus, X. albilineans exhibits distinctive genomic characteristics including the presence of significant genome erosion, a non- ... ...

    Abstract Xanthomonas albilineans is the bacterium responsible for leaf scald, a lethal disease of sugarcane. Within the Xanthomonas genus, X. albilineans exhibits distinctive genomic characteristics including the presence of significant genome erosion, a non-ribosomal peptide synthesis (NRPS) locus involved in albicidin biosynthesis, and a type 3 secretion system (T3SS) of the Salmonella pathogenicity island-1 (SPI-1) family. We sequenced two X. albilineans-like strains isolated from unusual environments, i.e., from dew droplets on sugarcane leaves and from the wild grass Paspalum dilatatum, and compared these genomes sequences with those of two strains of X. albilineans and three of Xanthomonas sacchari. Average nucleotide identity (ANI) and multi-locus sequence analysis (MLSA) showed that both X. albilineans-like strains belong to a new species close to X. albilineans that we have named "Xanthomonas pseudalbilineans". X. albilineans and "X. pseudalbilineans" share many genomic features including (i) the lack of genes encoding a hypersensitive response and pathogenicity type 3 secretion system (Hrp-T3SS), and (ii) genome erosion that probably occurred in a common progenitor of both species. Our comparative analyses also revealed specific genomic features that may help X. albilineans interact with sugarcane, e.g., a PglA endoglucanase, three TonB-dependent transporters and a glycogen metabolism gene cluster. Other specific genomic features found in the "X. pseudalbilineans" genome may contribute to its fitness and specific ecological niche.
    Language English
    Publishing date 2015-07-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527218-4
    ISSN 2073-4425
    ISSN 2073-4425
    DOI 10.3390/genes6030714
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  9. Article ; Online: Total synthesis of albicidin: a lead structure from Xanthomonas albilineans for potent antibacterial gyrase inhibitors.

    Kretz, Julian / Kerwat, Dennis / Schubert, Vivien / Grätz, Stefan / Pesic, Alexander / Semsary, Siamak / Cociancich, Stéphane / Royer, Monique / Süssmuth, Roderich D

    Angewandte Chemie (International ed. in English)

    2015  Volume 54, Issue 6, Page(s) 1969–1973

    Abstract: The peptide antibiotic albicidin, which is synthesized by the plant pathogenic bacterium Xanthomonas albilineans, displays remarkable antibacterial activity against various Gram-positive and Gram-negative microorganisms. The low amounts of albicidin ... ...

    Abstract The peptide antibiotic albicidin, which is synthesized by the plant pathogenic bacterium Xanthomonas albilineans, displays remarkable antibacterial activity against various Gram-positive and Gram-negative microorganisms. The low amounts of albicidin obtainable from the producing organism or through heterologous expression are limiting factors in providing sufficient material for bioactivity profiling and structure-activity studies. Therefore, we developed a convergent total synthesis route toward albicidin. The unexpectedly difficult formation of amide bonds between the aromatic amino acids was achieved through a triphosgene-mediated coupling strategy. The herein presented synthesis of albicidin confirms the previously determined chemical structure and underlines the extraordinary antibacterial activity of this compound. The synthetic protocol will provide multigram amounts of albicidin for further profiling of its drug properties.
    MeSH term(s) Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; DNA Gyrase/drug effects ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Molecular Structure ; Organic Chemicals/chemistry ; Organic Chemicals/pharmacology ; Xanthomonas/chemistry
    Chemical Substances Anti-Bacterial Agents ; Enzyme Inhibitors ; Organic Chemicals ; albicidin (96955-97-4) ; DNA Gyrase (EC 5.99.1.3)
    Language English
    Publishing date 2015-02-02
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201409584
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  10. Article ; Online: The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides.

    Vieweg, Laura / Kretz, Julian / Pesic, Alexander / Kerwat, Dennis / Grätz, Stefan / Royer, Monique / Cociancich, Stéphane / Mainz, Andi / Süssmuth, Roderich D

    Journal of the American Chemical Society

    2015  Volume 137, Issue 24, Page(s) 7608–7611

    Abstract: The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various ... ...

    Abstract The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria. The bacterium Pantoea dispersa expresses the hydrolase AlbD, conferring natural resistance against albicidin. We show that AlbD is a novel type of endopeptidase that catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimicrobial activity. Additionally, we determined the minimal cleavage motif of AlbD with substrates derived by chemical synthesis. Our results clearly identify AlbD as a unique endopeptidase that is the first member of a new subfamily of peptidases. Our findings provide the molecular basis for a natural detoxification mechanism, potentially rendering a new tool in biological chemistry approaches.
    MeSH term(s) Anti-Bacterial Agents/metabolism ; Anti-Bacterial Agents/pharmacology ; Drug Resistance, Bacterial ; Enterobacteriaceae Infections/drug therapy ; Enterobacteriaceae Infections/microbiology ; Humans ; Hydrolysis ; Organic Chemicals/metabolism ; Organic Chemicals/pharmacology ; Pantoea/drug effects ; Pantoea/enzymology ; Serine Endopeptidases/metabolism ; Xanthomonas/metabolism
    Chemical Substances Anti-Bacterial Agents ; Organic Chemicals ; albicidin (96955-97-4) ; Serine Endopeptidases (EC 3.4.21.-)
    Language English
    Publishing date 2015-06-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.5b04099
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