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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Petya KRASTEVA : Biologie Structurale des Biofilms



  • P. V. Krasteva, J. Bernal-Bayard, L. Travier, F. A. Martin, P. - A. Kaminski, G. Karimova, R. Fronzes, et J. - M. Ghigo, « Insights into the structure and assembly of a bacterial cellulose secretion system », Nature Communications, vol. 8, nᵒ 1, p. 2065, déc. 2017.
    Résumé : Secreted exopolysaccharides present important determinants for bacterial biofilm formation, survival, and virulence. Cellulose secretion typically requires the concerted action of a c-di-GMP-responsive inner membrane synthase (BcsA), an accessory membrane-anchored protein (BcsB), and several additional Bcs components. Although the BcsAB catalytic duo has been studied in great detail, its interplay with co-expressed subunits remains enigmatic. Here we show that E. coli Bcs proteins partake in a complex protein interaction network. Electron microscopy reveals a stable, megadalton-sized macromolecular assembly, which encompasses most of the inner membrane and cytosolic Bcs components and features a previously unobserved asymmetric architecture. Heterologous reconstitution and mutational analyses point toward a structure-function model, where accessory proteins regulate secretion by affecting both the assembly and stability of the system. Altogether, these results lay the foundation for more comprehensive models of synthase-dependent exopolysaccharide secretion in biofilms and add a sophisticated secretory nanomachine to the diverse bacterial arsenal for virulence and adaptation.
    Mots-clés : B3S, SBB.

  • P. V. Krasteva et H. Sondermann, « Versatile modes of cellular regulation via cyclic dinucleotides », Nature Chemical Biology, vol. 13, nᵒ 4, p. 350-359, mars 2017.

  • B. Y. Matsuyama, P. V. Krasteva, et M. V. A. S. Navarro, « Isothermal Titration Calorimetry to Determine Apparent Dissociation Constants (K d) and Stoichiometry of Interaction (n) of C-di-GMP Binding Proteins », Methods in Molecular Biology (Clifton, N.J.), vol. 1657, p. 403-416, 2017.
    Résumé : Isothermal titration calorimetry (ITC) is a commonly used biophysical technique that enables the quantitative characterization of intermolecular interactions in solution. Based on enthalpy changes (ΔH) upon titration of the binding partner (e.g., a small-molecule ligand such as c-di-GMP) to the molecule of interest (e.g., a receptor protein), the resulting binding isotherms provide information on the equilibrium association/dissociation constants (K a, K d) and stoichiometry of binding (n), as well as on changes in the Gibbs free energy (ΔG) and entropy (ΔS) along the interaction. Here we present ITC experiments used for the characterization of c-di-GMP binding proteins and discuss advantages and potential caveats in the interpretation of results.
    Mots-clés : B3S, Binding stoichiometry, c-di-GMP, C-di-GMP sensor proteins, Dissociation constant (K d), Intermolecular interactions, isothermal titration calorimetry (ITC), Receptor–ligand interactions, SBB.
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- Matsuyama BY*, Krasteva PV*, Baraquet C, Harwood CS, Sondermann H, Navarro MV. Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa. Proc Natl Acad Sci U S A. 2016 Jan 12 ; 113(2):E209-18

- Laurenceau R*, Krasteva PV*, ✉, Diallo A, Ouarti S, Duchateau M, Malosse C, Chamot-Rooke J, Fronzes R ✉. Conserved Streptococcus pneumoniae spirosomes suggest a single type of transformation pilus in competence. PLoS Pathog. 2015 Apr 15 ;11(4):e1004835

- Goyal P, Krasteva PV, Van Gerven N, Gubellini F, Van den Broeck I, Troupiotis-Tsaïlaki A, Jonckheere W, Péhau-Arnaudet G, Pinkner JS, Chapman MR, Hultgren SJ, Howorka S, Fronzes R, Remaut H. Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature. 2014 Dec 11 ;516(7530):250-3
- Krasteva PV. CRISPR snapshots of a gene-editing tool. Nat Methods. 2014 Apr ;11(4):365
- Krasteva PV. Zooming in on nuclear logistics. Nat Methods. 2014 Feb ;11(2):126-7

- Krasteva PV, Giglio KM, Sondermann H. Sensing the messenger : the diverse ways that bacteria signal through c-di-GMP. Protein Sci. 2012 Jul ;21(7):929-48
- Krasteva PV. DNA nanoLEGOlogy. Nat Methods. 2012 Jul ;9(7):640-1
- Krasteva PV. RNA structures. Nat Methods. 2012 Jan ;9 (1), 38-38

Avant 2012
- Krasteva PV. Wholesome proteomics. Nat Methods. 2011 Dec ;8(12):1002
- Krasteva PV. Molecular matchmaking for neural control. Nat Methods. 2011 Nov ;8(11):898
- Krasteva PV. Clarifying brain structure, literally. Nat Methods. 2011 ;8(10):793
- Krasteva PV. Bacterial electrophysiology brought to light. Nat Methods. 2011 Sep ;8(9):714
- Krasteva PV. Taming crystals’ whimsy. Nat Methods. 2011 Aug ;8(8):622
- Navarro MV*, Newell PD*, Krasteva PV*, Chatterjee D*, Madden DR, O’Toole GA, Sondermann H. Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis. PLoS Biol. 2011 Feb 1 ;9(2):e1000588
- Krasteva PV, Fong JC, Shikuma NJ, Beyhan S, Navarro MV, Yildiz FH, Sondermann H. Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Science. 2010 Feb 12 ;327(5967):866-8
- De N*, Navarro MV*, Wang Q*, Krasteva PV*, Sondermann H. Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation. Methods Enzymol. 2010 ;471:161-84
- De N, Pirruccello M, Krasteva PV, Bae N, Raghavan RV, Sondermann H. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS Biol. 2008 Mar 25 ;6(3):e67

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