Search results for: Severine Zirah

Items from 1 to 19 out of 19 results

article

Phenomic and genomic approaches to studying the inhibition of multiresistant Salmonella enterica by microcin J25

Laila Ben Said, Jean‐Guillaume Emond‐Rheault, Samira Soltani, Sofiane Telhig, more

Environmental Microbiology > 22 > 7 > 2907 - 2920

In livestock production, antibiotics are used to promote animal growth, control infections and thereby increase profitability. This practice has led to the emergence of multiresistant bacteria such as Salmonella, of which some serovars are disseminated in the environment. The objective of this study is to evaluate microcin J25 as an inhibitor of Salmonella enterica serovars of various origins including...

article

Evidence of Cis/Trans-Isomerization at Pro7/Pro16 in the Lasso Peptide Microcin J25

Kevin Jeanne Dit Fouque, Julian D. Hegemann, Séverine Zirah, Sylvie Rebuffat, more

Journal of The American Society for Mass Spectrometry > 2019 > 30 > 6 > 1038-1045

Microcin J25 is a ribosomal synthesized and post-translationally modified peptide (RiPP) characterized by a mechanically interlocked topology called the lasso fold. This structure provides microcin J25 a potent antimicrobial activity resulting from internalization via the siderophore receptor FhuA and further inhibition of the RNA polymerase. In the present work, nuclear magnetic resonance (NMR) and...

article

Structural signatures of the class III lasso peptide BI-32169 and the branched-cyclic topoisomers using trapped ion mobility spectrometry–mass spectrometry and tandem mass spectrometry

Kevin Jeanne Dit Fouque, Vikash Bisram, Julian D. Hegemann, Séverine Zirah, more

Analytical and Bioanalytical Chemistry > 2019 > 411 > 24 > 6287-6296

Lasso peptides are a class of bioactive ribosomally synthesized and post-translationally modified peptides (RiPPs) characterized by a mechanically interlocked topology, where the C-terminal tail of the peptide is threaded and trapped within an N-terminal macrolactam ring. BI-32169 is a class III lasso peptide containing one disulfide bond that further stabilizes the lasso structure. In contrast to...

article

Signatures of Mechanically Interlocked Topology of Lasso Peptides by Ion Mobility–Mass Spectrometry: Lessons from a Collection of Representatives

Kevin Jeanne Dit Fouque, Hélène Lavanant, Séverine Zirah, Julian D. Hegemann, more

Journal of The American Society for Mass Spectrometry > 2017 > 28 > 2 > 315-322

Lasso peptides are characterized by a mechanically interlocked structure, where the C-terminal tail of the peptide is threaded and trapped within an N-terminal macrolactam ring. Their compact and stable structures have a significant impact on their biological and physical properties and make them highly interesting for drug development. Ion mobility - mass spectrometry (IM-MS) has shown to be effective...

chapter

Post-Translational Modification and folding of A Lasso-Type Gene-Encoded Antimicrobial Peptide Require Two Enzymes only in Escherichia coli

Sophie Duquesne, Delphine Destoumieux-Garzón, Séverine Zirah, Thomas A. Knappe, more

Advances in Experimental Medicine and Biology > Peptides for Youth > Folding, Recognition, and Catalysis: dedicated to Elkan Blout > 35-36

chapter

Biosynthesis of Siderophore-Peptides, A Class of Potent Antimicrobial Peptides from Enterobacteria, Requires Two Precursors

Gaëlle Vassiliadis, Jean Peduzzi, Delphine Destoumieux-Garzón, Séverine Zirah, more

Advances in Experimental Medicine and Biology > Peptides for Youth > Folding, Recognition, and Catalysis: dedicated to Elkan Blout > 33-34

article

Electron detachment/photodetachment dissociation of lasso peptides

Marie Pérot-Taillandier, Carlos Afonso, Quentin Enjalbert, Rodolphe Antoine, more

International Journal of Mass Spectrometry > 2015 > 390 > C > 91-100

Lasso peptides are bioactive peptides produced by bacteria, characterized by a mechanically interlocked topology where the C-terminal tail of the peptide is threaded through and trapped within an N-terminal macrolactam ring. The structural characterization of lasso peptides and differentiation from their unthreaded topoisomers by mass spectrometry are challenging tasks. We previously explored the...

article

Gas‐phase conformations of capistruin – comparison of lasso, branched‐cyclic and linear topologies

Kevin Jeanne Dit Fouque, Hélène Lavanant, Séverine Zirah, Jérôme Lemoine, more

Rapid Communications in Mass Spectrometry > 29 > 15 > 1411 - 1419

RationaleCapistruin is a peptide synthesized by Burkholderia thailandensis E264, which displays a lasso topology. This knot‐like structure confers interesting properties to peptides (e.g. antibacterial). Therefore, it is important to evaluate the sensitivity of structural characterization methods to such topological constraints. MethodsIon mobility mass spectrometry (IMS‐MS) experiments, using both...

article

Sponging up metals: Bacteria associated with the marine sponge Spongia officinalis

Cléa Bauvais, Séverine Zirah, Laurie Piette, Florence Chaspoul, more

Marine Environmental Research > 2015 > 104 > Complete > 20-30

The present study explored the bacteria of the sponge Spongia officinalis in a metal-polluted environment, using PCR-DGGE fingerprinting, culture-dependent approaches and in situ hybridization. The sponge samples collected over three consecutive years in the Western Mediterranean Sea contained high concentrations of zinc, nickel, lead and copper determined by ICP-MS. DGGE signatures indicated a sponge...

article

Thiazole‐Based γ‐Building Blocks as Reverse‐Turn Mimetic to Design a Gramicidin S Analogue: Conformational and Biological Evaluation

Baptiste Legrand, Loïc Mathieu, Aurélien Lebrun, Soahary Andriamanarivo, more

Chemistry – A European Journal > 20 > 22 > 6713 - 6720

This paper describes the ability of a new class of heterocyclic γ‐amino acids named ATCs (4‐amino(methyl)‐1,3‐thiazole‐5‐carboxylic acids) to induce turns when included in a tetrapeptide template. Both hybrid Ac‐Val‐(R or S)‐ATC‐Ile‐Ala‐NH₂ sequences were synthesized and their conformations were studied by circular dichroism, NMR spectroscopy, MD simulations, and DFT calculations. It was demonstrated...

article

Prompt and Slow Electron‐Detachment‐Dissociation/Electron‐Photodetachment‐Dissociation of a 21‐Mer Peptide

Marie Pérot‐Taillandier, Séverine Zirah, Quentin Enjalbert, Rodolphe Antoine, more

Chemistry – A European Journal > 19 > 1 > 350 - 357

Electron detachment dissociation (EDD) and electron photodetachment dissociation (EPD) are relatively new dissociation methods that involve electron detachment followed by radical‐driven dissociation from multiply deprotonated species. EDD yields prompt dissociation whereas only electron detachment is obtained by EPD; subsequent vibrational activation of the charge‐reduced radical anion is required...

article

Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides

Séverine Zirah, Carlos Afonso, Uwe Linne, Thomas A. Knappe, more

Journal of The American Society for Mass Spectrometry > 2011 > 22 > 3 > 467-479

Lasso peptides constitute a class of bioactive peptides sharing a knotted structure where the C-terminal tail of the peptide is threaded through and trapped within an N-terminal macrolactam ring. The structural characterization of lasso structures and differentiation from their unthreaded topoisomers is not trivial and generally requires the use of complementary biochemical and spectroscopic methods...

article

Collision Induced Dissociation-Based Characterization of Nucleotide Peptides: Fragmentation Patterns of Microcin C7-C51, an Antimicrobial Peptide Produced by Escherichia coli

Vanessa W. Petit, Séverine Zirah, Sylvie Rebuffat, Jean-Claude Tabet

Journal of the American Society for Mass Spectrometry > 2008 > 19 > 8 > 1187-1198

Covalent protein-nucleic acid conjugates form an original class of compounds that occur in nature or can be generated in vitro through cross-linking to investigate domains involved in protein/nucleic acid interactions. Their mass spectrometry fragmentation patterns are poorly characterized. We have used electrospray-ionization mass spectrometry (ESI-MS) combined with collision-induced dissociation...

article

Collision induced dissociation-based characterization of nucleotide peptides: Fragmentation patterns of microcin C7–C51, an antimicrobial peptide produced by Escherichia coli

Vanessa W. Petit, Séverine Zirah, Sylvie Rebuffat, Jean-Claude Tabet

Journal of The American Society for Mass Spectrometry > 2008 > 19 > 8 > 1187-1198

article

Two Enzymes Catalyze the Maturation of a Lasso Peptide in Escherichia coli

Sophie Duquesne, Delphine Destoumieux-Garzón, Séverine Zirah, Christophe Goulard, more

Chemistry & Biology > 2007 > 14 > 7 > 793-803

Microcin J25 (MccJ25) is a gene-encoded lasso peptide secreted by Escherichia coli which exerts a potent antibacterial activity by blocking RNA polymerase. Here we demonstrate that McjB and McjC, encoded by genes in the MccJ25 gene cluster, catalyze the maturation of MccJ25. Requirement for both McjB and McjC was shown by gene inactivation and complementation assays. Furthermore, the conversion of...

article

Statistical Search Space Reduction and Two-Dimensional Data Display Approaches for UPLC−MS in Biomarker Discovery and Pathway Analysis

Derek J. Crockford, John C. Lindon, Olivier Cloarec, Robert S. Plumb, more

Analytical Chemistry > 2006 > 78 > 13 > 4398 - 4408

article

Statistical Heterospectroscopy, an Approach to the Integrated Analysis of NMR and UPLC-MS Data Sets: Application in Metabonomic Toxicology Studies

Derek J. Crockford, Elaine Holmes, John C. Lindon, Robert S. Plumb, more

Analytical Chemistry > 2006 > 78 > 2 > 363 - 371

article

Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies

Séverine Zirah, Raluca Stefanescu, Marilena Manea, Xiaodan Tian, more

Biochemical and Biophysical Research Communications > 2004 > 321 > 2 > 324-328

Amyloid plaques associated to Alzheimer’s disease present a high content of zinc ions. We previously showed that the N-terminal region of the amyloid peptide Aβ constitutes an autonomous zinc-binding domain. This region encompasses the previously identified epitope Aβ(4–10) targeted by antibodies capable to reduce amyloid deposition, but the influence of Aβ/Zn binding on the epitope recognition remains...

article

Zinc Binding to Alzheimer's Aβ(1–16) Peptide Results in Stable Soluble Complex

Sergey A. Kozin, Séverine Zirah, Sylvie Rebuffat, Gaston Hui Bon Hoa, more

Biochemical and Biophysical Research Communications > 2001 > 285 > 4 > 959-964

Aggregation of the human amyloid β-peptide (Aβ) into insoluble plaques is a key event in Alzheimer's disease. Zinc sharply accelerates the Aβ aggregation in vitro, and the Aβ region 6–28 was suggested to be the obligatory zinc binding site. However, time-dependent aggregation of the zinc-bound Aβ species investigated so far prevented their structural analysis. By using CD spectroscopy, we have shown...

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