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1. Calcium-dependent disorder-to-order transitions are central to the secretion and folding of the CyaA toxin of Bordetella pertussis, the causative agent of whooping cough

Author

O'Brien, Darragh P., Perez, Ana Cristina Sotomayor, Karst, Johanna, Cannella, Sara E., Enguéné, Véronique Yvette Ntsogo, Hessel, Audrey, Raoux-Barbot, Dorothée, Voegele, Alexis, Subrini, Orso, Davi, Marilyne, Guijarro, J. Inaki, Raynal, Bertrand, Baron, Bruno, England, Patrick, Hernandez, Belen, Ghomi, Mahmoud, Hourdel, Véronique, Malosse, Christian, Chamot-Rooke, Julia, Vachette, Patrice, Durand, Dominique, Brier, Sébastien, Ladant, Daniel, and Chenal, Alexandre

Published
2018
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4. CyaA toxin translocation across host cell plasma membrane requires hijacking of calmodulin

Author

Voegele, Alexis, primary, Sadi, Mirko, additional, O'Brien, Darragh P., additional, Gehan, Pauline, additional, Hoos, Sylviane, additional, Brûlé, Sébastien, additional, Raynal, Bertrand, additional, Mechaly, Ariel, additional, Haouz, Ahmed, additional, Rodriguez, Nicolas, additional, Vachette, Patrice, additional, Durand, Dominique, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2023
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6. Cell invasion involves membrane-active and calmodulin-binding properties of the CyaA toxin translocation domain

Author

Voegele, Alexis, primary, Sadi, Mirko, additional, O’Brien, Darragh P., additional, Gehan, Pauline, additional, Raoux-Barbot, Dorothée, additional, Hoos, Sylviane, additional, Brûlé, Sébastien, additional, Raynal, Bertrand, additional, Haouz, Ahmed, additional, Rodriguez, Nicolas, additional, Vachette, Patrice, additional, Durand, Dominique, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2022
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7. A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells

Author

Voegele, Alexis, primary, Sadi, Mirko, additional, O'Brien, Darragh Patrick, additional, Gehan, Pauline, additional, Raoux‐Barbot, Dorothée, additional, Davi, Maryline, additional, Hoos, Sylviane, additional, Brûlé, Sébastien, additional, Raynal, Bertrand, additional, Weber, Patrick, additional, Mechaly, Ariel, additional, Haouz, Ahmed, additional, Rodriguez, Nicolas, additional, Vachette, Patrice, additional, Durand, Dominique, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2021
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8. A high-affinity calmodulin-binding site in the CyaA toxin translocation domain is essential for invasion into eukaryotic cells

Author

Voegele, Alexis, primary, Sadi, Mirko, additional, O’Brien, Darragh P, additional, Gehan, Pauline, additional, Raoux-Barbot, Dorothée, additional, Davi, Maryline, additional, Hoos, Sylviane, additional, Brûlé, Sébastien, additional, Raynal, Bertrand, additional, Weber, Patrick, additional, Mechaly, Ariel, additional, Haouz, Ahmed, additional, Rodriguez, Nicolas, additional, Vachette, Patrice, additional, Durand, Dominique, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2020
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9. Disorder-To-Order Transitions and Post-Translational Acylation Control the Folding and Activity of the Bordetella Pertussis CyaA Toxin

Author

O'Brien, Darragh P., primary, Voegele, Alexis, additional, Raoux-Barbot, Dorothée, additional, Davi, Marilyne, additional, Cannella, Sara, additional, Douché, Thibaut, additional, Matondo, Mariette, additional, Durand, Dominique, additional, Vachette, Patrice, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2020
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10. Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation inCorynebacterium glutamicum

Author

Sogues, Adrià, primary, Martinez, Mariano, additional, Gaday, Quentin, additional, Ben-Assaya, Mathilde, additional, Graña, Martin, additional, Voegele, Alexis, additional, VanNieuwenhze, Michael, additional, England, Patrick, additional, Haouz, Ahmed, additional, Chenal, Alexandre, additional, Trépout, Sylvain, additional, Duran, Rosario, additional, Wehenkel, Anne Marie, additional, and Alzari, Pedro, additional

Published
2019
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14. Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis

Author

O’Brien, Darragh P., Durand, Dominique, Voegele, Alexis, Hourdel, Véronique, Davi, Marilyne, Chamot-Rooke, Julia, Vachette, Patrice, Brier, Sébastien, Ladant, Daniel, Chenal, Alexandre, Département de Biologie structurale et Chimie - Department of Structural Biology and Chemistry, Institut Pasteur [Paris], Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology (UTechS MSBio), Institut Pasteur [Paris]-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Fondation pour la Recherche Médicale (FRM) https://www.frm.org/ (grant number DBS 20140930771). Received By DOB, AV, MD, DL, and AC.. DOB, AV, VH, MD, JCR, SB, DL, and AC. Region Ile de France (grant number DIM MalInf 2016). AV and AC. CNRS. DOB, DD, AV, VH, MD, JCR, PV, SB, DL, and AC. Institut Pasteur (grant number PasteurInnoV15006-01A and PTR451). DOB and AC., ANR-11-EQPX-0008,CACSICE,Centre d'analyse de systèmes complexes dans les environnements complexes(2011), Institut Pasteur [Paris] (IP), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), and Institut Pasteur [Paris] (IP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Bioinformatics, Protein Conformation, QH301-705.5, Toxic Agents, Lyases, Toxicology, Pathology and Laboratory Medicine, Research and Analysis Methods, Biochemistry, Catalysis, Bordetella pertussis, Mass Spectrometry, Small-Angle Scattering, Scattering, Database and Informatics Methods, Signs and Symptoms, Calmodulin, Sequence Motif Analysis, Diagnostic Medicine, Catalytic Domain, Scattering, Small Angle, Medicine and Health Sciences, Cyclic AMP, Solid State Physics, Toxins, Edema, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Calcium Signaling, Biology (General), Crystallography, Physics, Circular Dichroism, Biology and Life Sciences, Proteins, Deuterium Exchange Measurement, Condensed Matter Physics, Enzymes, Chemistry, Physical Sciences, Crystal Structure, Enzymology, Adenylate Cyclase Toxin, Sequence Analysis, Adenylyl Cyclase, Synchrotrons, Research Article, Protein Binding
Abstract

Once translocated into the cytosol of target cells, the catalytic domain (AC) of the adenylate cyclase toxin (CyaA), a major virulence factor of Bordetella pertussis, is potently activated by binding calmodulin (CaM) to produce supraphysiological levels of cAMP, inducing cell death. Using a combination of small-angle X-ray scattering (SAXS), hydrogen/deuterium exchange mass spectrometry (HDX-MS), and synchrotron radiation circular dichroism (SR-CD), we show that, in the absence of CaM, AC exhibits significant structural disorder, and a 75-residue-long stretch within AC undergoes a disorder-to-order transition upon CaM binding. Beyond this local folding, CaM binding induces long-range allosteric effects that stabilize the distant catalytic site, whilst preserving catalytic loop flexibility. We propose that the high enzymatic activity of AC is due to a tight balance between the CaM-induced decrease of structural flexibility around the catalytic site and the preservation of catalytic loop flexibility, allowing for fast substrate binding and product release. The CaM-induced dampening of AC conformational disorder is likely relevant to other CaM-activated enzymes., Author summary Calmodulin is a widespread and highly conserved protein that interacts with a wide variety of eukaryotic proteins and enzymes, controlling their activities in response to calcium. The adenylate cyclase toxin (CyaA) of Bordetella pertussis, the causative agent of whooping cough, is one such calmodulin target. Once transported across the plasma membrane of eukaryotic cells, the catalytic domain (AC) of CyaA is activated by calmodulin, producing high levels of cAMP, which can induce cell death. We use an integrative structural biology approach combining several biophysical techniques to characterize the structural rearrangements in AC upon calmodulin binding and to elucidate their relationship to CyaA activation. We show that a disordered stretch of 75 amino acid residues in AC serves as a bait for calmodulin capture. Binding induces significant folding within this region, a prerequisite for CyaA activation. Calmodulin binding promotes the stabilization of the distant catalytic site, whilst maintaining its catalytic loop in a flexible and exposed state. Both phenomena contribute to the high enzymatic activity of AC, allowing for fast substrate binding and cAMP release. The calmodulin-induced reduction of AC conformational disorder is likely relevant to other calmodulin-activated enzymes.

Published
2017

15. Bacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes

Author

Akendengue, Lurlène, Trépout, Sylvain, Graña, Martín, Voegele, Alexis, Janke, Carsten, Raynal, Bertrand, Chenal, Alexandre, Marco, Sergio, Wehenkel, Anne Marie, Université Paris-Sud - Paris 11 (UP11), Institut Curie [Paris], Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP), Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Biophysique Moléculaire (Plate-forme), This work was supported by the Institut Curie, the Institut Pasteur, the CNRS, INSERM, DIM MALINF and the French National Research Agency., ANR-12-PDOC-0021,HetTub,Mécanismes moléculaires et fonctions de l'hétérogenéité de la tubuline(2012), ANR-10-IDEX-0001,PSL,Paris Sciences et Lettres(2010), ANR-10-EQPX-0038,MIMETIS,Microscopie Interférométrique et Microscopie Electronique en Transmission In Situ(2010), and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

Subjects
Membrane Lipids, Bacterial Proteins, Verrucomicrobia, [SDV]Life Sciences [q-bio], Cryoelectron tomography, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, macromolecular substances, Cellular microbiology, Microtubules, Cytoskeleton, Article, Cytoskeletal proteins
Abstract

International audience; Bacterial kinesin light chain is a TPR domain-containing protein encoded by the bklc gene, which co-localizes with the bacterial tubulin (btub) genes in a conserved operon in Prosthecobacter. Btub heterodimers show high structural homology with eukaryotic tubulin and assemble into head-to-tail protofilaments. Intriguingly, Bklc is homologous to the light chain of the microtubule motor kinesin and could thus represent an additional eukaryotic-like cytoskeletal element in bacteria. Using biochemical characterization as well as cryo-electron tomography we show here that Bklc interacts specifically with Btub protofilaments, as well as lipid vesicles and could thus play a role in anchoring the Btub filaments to the membrane protrusions in Prosthecobacter where they specifically localize in vivo. This work sheds new light into possible ways in which the microtubule cytoskeleton may have evolved linking precursors of microtubules to the membrane via the kinesin moiety that in today's eukaryotic cytoskeleton links vesicle-packaged cargo to microtubules.

Published
2017

16. Translocation and calmodulin-activation of the adenylate cyclase toxin (CyaA) ofBordetella pertussis

Author

Voegele, Alexis, primary, O’Brien, Darragh P, additional, Subrini, Orso, additional, Sapay, Nicolas, additional, Cannella, Sara E, additional, Enguéné, Véronique Yvette Ntsogo, additional, Hessel, Audrey, additional, Karst, Johanna, additional, Hourdel, Véronique, additional, Perez, Ana Cristina Sotomayor, additional, Davi, Marilyne, additional, Veneziano, Rémi, additional, Chopineau, Joel, additional, Vachette, Patrice, additional, Durand, Dominique, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2018
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22. Translocation and calmodulin-activation of the adenylate cyclase toxin (CyaA) of Bordetella pertussis.

Author

Voegele, Alexis, O'Brien, Darragh P, Subrini, Orso, Sapay, Nicolas, Cannella, Sara E, Enguéné, Véronique Yvette Ntsogo, Hessel, Audrey, Karst, Johanna, Hourdel, Véronique, Perez, Ana Cristina Sotomayor, Davi, Marilyne, Veneziano, Rémi, Chopineau, Joel, Vachette, Patrice, Durand, Dominique, Brier, Sébastien, Ladant, Daniel, and Chenal, Alexandre

Subjects
*ADENYLATE cyclase, *BORDETELLA pertussis, *WHOOPING cough, *CATALYTIC domains, *RESPIRATORY infections
Abstract

The adenylate cyclase toxin (CyaA) is a multi-domain protein secreted by Bordetella pertussis, the causative agent of whooping cough. CyaA is involved in the early stages of respiratory tract colonization by Bordetella pertussis. CyaA is produced and acylated in the bacteria, and secreted via a dedicated secretion system. The cell intoxication process involves a unique mechanism of transport of the CyaA toxin catalytic domain (ACD) across the plasma membrane of eukaryotic cells. Once translocated, ACD binds to and is activated by calmodulin and produces high amounts of cAMP, subverting the physiology of eukaryotic cells. Here, we review our work on the identification and characterization of a critical region of CyaA, the translocation region, required to deliver ACD into the cytosol of target cells. The translocation region contains a segment that exhibits membrane-active properties, i.e. is able to fold upon membrane interaction and permeabilize lipid bilayers. We proposed that this region is required to locally destabilize the membrane, decreasing the energy required for ACD translocation. To further study the translocation process, we developed a tethered bilayer lipid membrane (tBLM) design that recapitulate the ACD transport across a membrane separating two hermetic compartments. We showed that ACD translocation is critically dependent on calcium, membrane potential, CyaA acylation and on the presence of calmodulin in the trans compartment. Finally, we describe how calmodulin-binding triggers key conformational changes in ACD, leading to its activation and production of supraphysiological concentrations of cAMP. [ABSTRACT FROM AUTHOR]

Published
2018
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23. Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis.

Author

O'Brien DP, Durand D, Voegele A, Hourdel V, Davi M, Chamot-Rooke J, Vachette P, Brier S, Ladant D, and Chenal A

Subjects
Adenylate Cyclase Toxin metabolism, Adenylate Cyclase Toxin physiology, Bordetella pertussis pathogenicity, Calcium Signaling, Calmodulin metabolism, Calmodulin physiology, Catalysis, Catalytic Domain, Circular Dichroism, Cyclic AMP metabolism, Deuterium Exchange Measurement, Mass Spectrometry, Models, Molecular, Protein Binding, Protein Conformation, Scattering, Small Angle, Synchrotrons, Adenylate Cyclase Toxin chemistry, Bordetella pertussis chemistry, Calmodulin chemistry
Abstract

Once translocated into the cytosol of target cells, the catalytic domain (AC) of the adenylate cyclase toxin (CyaA), a major virulence factor of Bordetella pertussis, is potently activated by binding calmodulin (CaM) to produce supraphysiological levels of cAMP, inducing cell death. Using a combination of small-angle X-ray scattering (SAXS), hydrogen/deuterium exchange mass spectrometry (HDX-MS), and synchrotron radiation circular dichroism (SR-CD), we show that, in the absence of CaM, AC exhibits significant structural disorder, and a 75-residue-long stretch within AC undergoes a disorder-to-order transition upon CaM binding. Beyond this local folding, CaM binding induces long-range allosteric effects that stabilize the distant catalytic site, whilst preserving catalytic loop flexibility. We propose that the high enzymatic activity of AC is due to a tight balance between the CaM-induced decrease of structural flexibility around the catalytic site and the preservation of catalytic loop flexibility, allowing for fast substrate binding and product release. The CaM-induced dampening of AC conformational disorder is likely relevant to other CaM-activated enzymes.

Published
2017
Full Text
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24. Bacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes.

Author

Akendengue L, Trépout S, Graña M, Voegele A, Janke C, Raynal B, Chenal A, Marco S, and Wehenkel AM

Subjects
Bacterial Proteins chemistry, Cytoskeletal Proteins metabolism, Verrucomicrobia metabolism, Verrucomicrobia ultrastructure, Bacterial Proteins metabolism, Cytoskeleton metabolism, Membrane Lipids metabolism, Microtubules metabolism
Abstract

Bacterial kinesin light chain is a TPR domain-containing protein encoded by the bklc gene, which co-localizes with the bacterial tubulin (btub) genes in a conserved operon in Prosthecobacter. Btub heterodimers show high structural homology with eukaryotic tubulin and assemble into head-to-tail protofilaments. Intriguingly, Bklc is homologous to the light chain of the microtubule motor kinesin and could thus represent an additional eukaryotic-like cytoskeletal element in bacteria. Using biochemical characterization as well as cryo-electron tomography we show here that Bklc interacts specifically with Btub protofilaments, as well as lipid vesicles and could thus play a role in anchoring the Btub filaments to the membrane protrusions in Prosthecobacter where they specifically localize in vivo. This work sheds new light into possible ways in which the microtubule cytoskeleton may have evolved linking precursors of microtubules to the membrane via the kinesin moiety that in today's eukaryotic cytoskeleton links vesicle-packaged cargo to microtubules.

Published
2017
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