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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Pierre DORLET : Stress Oxydant et Détoxication

Publications de l’équipe


  • M. David, C. Lebrun, T. Duguet, F. Talmont, R. Beech, S. Orlowski, F. André, R. K. Prichard, et A. Lespine, « Structural model, functional modulation by ivermectin and tissue localization of Haemonchus contortus P-glycoprotein-13 », International Journal for Parasitology. Drugs and Drug Resistance, vol. 8, nᵒ 1, p. 145-157, avr. 2018.
    Résumé : Haemonchus contortus, one of the most economically important parasites of small ruminants, has become resistant to the anthelmintic ivermectin. Deciphering the role of P-glycoproteins in ivermectin resistance is desirable for understanding and overcoming this resistance. In the model nematode, Caenorhabditis elegans, P-glycoprotein-13 is expressed in the amphids, important neuronal structures for ivermectin activity. We have focused on its ortholog in the parasite, Hco-Pgp-13. A 3D model of Hco-Pgp-13, presenting an open inward-facing conformation, has been constructed by homology with the Cel-Pgp-1 crystal structure. In silico docking calculations predicted high affinity binding of ivermectin and actinomycin D to the inner chamber of the protein. Following in vitro expression, we showed that ivermectin and actinomycin D modulated Hco-Pgp-13 ATPase activity with high affinity. Finally, we found in vivo Hco-Pgp-13 localization in epithelial, pharyngeal and neuronal tissues. Taken together, these data suggest a role for Hco-Pgp-13 in ivermectin transport, which could contribute to anthelmintic resistance.
    Mots-clés : ABC transporters, B3S, Haemonchus contortus, Homology modeling, Ivermectin, LPSM, LSOD, Nematode, P-glycoprotein.

  • S. M. Kapetanaki, M. J. Burton, J. Basran, C. Uragami, P. C. E. Moody, J. S. Mitcheson, R. Schmid, N. W. Davies, P. Dorlet, M. H. Vos, N. M. Storey, et E. Raven, « A mechanism for CO regulation of ion channels », Nature Communications, vol. 9, nᵒ 1, p. 907, 2018.
    Résumé : Despite being highly toxic, carbon monoxide (CO) is also an essential intracellular signalling molecule. The mechanisms of CO-dependent cell signalling are poorly defined, but are likely to involve interactions with heme proteins. One such role for CO is in ion channel regulation. Here, we examine the interaction of CO with KATP channels. We find that CO activates KATP channels and that heme binding to a CXXHX16H motif on the SUR2A receptor is required for the CO-dependent increase in channel activity. Spectroscopic and kinetic data were used to quantify the interaction of CO with the ferrous heme-SUR2A complex. The results are significant because they directly connect CO-dependent regulation to a heme-binding event on the channel. We use this information to present molecular-level insight into the dynamic processes that control the interactions of CO with a heme-regulated channel protein, and we present a structural framework for understanding the complex interplay between heme and CO in ion channel regulation.
    Mots-clés : B3S, LSOD.

  • C. Orelle, C. Durmort, K. Mathieu, B. Duchêne, S. Aros, F. Fenaille, F. André, C. Junot, T. Vernet, et J. - M. Jault, « A multidrug ABC transporter with a taste for GTP », Scientific Reports, vol. 8, nᵒ 1, p. 2309, févr. 2018.
    Résumé : During the evolution of cellular bioenergetics, many protein families have been fashioned to match the availability and replenishment in energy supply. Molecular motors and primary transporters essentially need ATP to function while proteins involved in cell signaling or translation consume GTP. ATP-Binding Cassette (ABC) transporters are one of the largest families of membrane proteins gathering several medically relevant members that are typically powered by ATP hydrolysis. Here, a Streptococcus pneumoniae ABC transporter responsible for fluoroquinolones resistance in clinical settings, PatA/PatB, is shown to challenge this concept. It clearly favors GTP as the energy supply to expel drugs. This preference is correlated to its ability to hydrolyze GTP more efficiently than ATP, as found with PatA/PatB reconstituted in proteoliposomes or nanodiscs. Importantly, the ATP and GTP concentrations are similar in S. pneumoniae supporting the physiological relevance of GTP as the energy source of this bacterial transporter.
    Mots-clés : B3S, LSOD.


  • L. Benkaidali, F. André, G. Moroy, B. Tangour, F. Maurel, et M. Petitjean, « The Cytochrome P450 3A4 Has Three Major Conformations: New Clues to Drug Recognition by this Promiscuous Enzyme », Molecular Informatics, juill. 2017.
    Résumé : We computed the channels of the 3A4 isoform of the cytochrome P450 3A4 (CYP) on the basis of 24 crystal structures extracted from the Protein Data Bank (PDB). We identified three major conformations (denoted C, O1 and O2) using an enhanced version of the CCCPP software that we developed for the present work, while only two conformations (C and O(2) ) are considered in the literature. We established the flowchart of definition of these three conformations in function of the structural and physicochemical parameters of the ligand. The channels are characterized with qualitative and quantitative parameters, and not only with their surrounding secondary structures as it is usually done in the literature.
    Mots-clés : active site access channels, B3S, conformations, CYP 3A4 ligands, cytochromes P450, drug-drug interactions, LSOD.

  • M. Clémancey, T. Cantat, G. Blondin, J. - M. Latour, P. Dorlet, et G. Lefèvre, « Structural Insights into the Nature of Fe(0) and Fe(I) Low-Valent Species Obtained upon the Reduction of Iron Salts by Aryl Grignard Reagents », Inorganic Chemistry, vol. 56, nᵒ 7, p. 3834-3848, avr. 2017.
    Résumé : Mechanistic studies of the reduction of Fe(III) and Fe(II) salts by aryl Grignard reagents in toluene/tetrahydrofuran mixtures in the absence of a supporting ligand, as well as structural insights regarding the nature of the low-valent iron species obtained at the end of this reduction process, are reported. It is shown that several reduction pathways can be followed, depending on the starting iron precursor. We demonstrate, moreover, that these pathways lead to a mixture of Fe(0) and Fe(I) complexes regardless of the nature of the precursor. Mössbauer and (1)H NMR spectroscopies suggest that diamagnetic 16-electron bisarene complexes such as (η(4)-C6H5Me)2Fe(0) can be formed as major species (85% of the overall iron quantity). The formation of a η(6)-arene-ligated low-spin Fe(I) complex as a minor species (accounting for ca. 15% of the overall iron quantity) is attested by Mössbauer spectroscopy, as well as by continuous-wave electron paramagnetic resonance (EPR) and pulsed-EPR (HYSCORE) spectroscopies. The nature of the Fe(I) coordination sphere is discussed by means of isotopic labeling experiments and density functional theory calculations. It is shown that the most likely low-spin Fe(I) candidate obtained in these systems is a diphenylarene-stabilized species [(η(6)-C6H5Me)Fe(I)Ph2](-) exhibiting an idealized C2v topology. This enlightens the nature of the lowest valence states accommodated by iron during the reduction of Fe(III) and Fe(II) salts by aryl Grignard reagents in the absence of any additional coligand, which so far remained rather unknown. The reactivity of these low-valent Fe(I) and Fe(0) complexes in aryl-heteroaryl Kumada cross-coupling conditions has also been investigated, and it is shown that the zerovalent Fe(0) species can be used efficiently as a precursor in this reaction, whereas the Fe(I) oxidation state does not exhibit any reactivity.
    Mots-clés : B3S, LSOD.

  • L. Dhers, N. Pietrancosta, L. Ducassou, B. Ramassamy, J. Dairou, M. Jaouen, F. André, D. Mansuy, et J. - L. Boucher, « Spectral and 3D model studies of the interaction of orphan human cytochrome P450 2U1 with substrates and ligands », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1861, nᵒ 1, p. 3144-3153, 2017.

  • L. Ducassou, L. Dhers, G. Jonasson, N. Pietrancosta, J. - L. Boucher, D. Mansuy, et F. André, « Membrane-bound human orphan cytochrome P450 2U1: Sequence singularities, construction of a full 3D model, and substrate docking », Biochimie, vol. 140, p. 166-175, sept. 2017.
    Résumé : BACKGROUND: Human cytochrome P450 2U1 (CYP2U1) is an orphan CYP that exhibits several distinctive characteristics among the 57 human CYPs with a highly conserved sequence in almost all living organisms. METHODS: We compared its protein sequence with those of the 57 human CYPs and constructed a 3D structure of a full-length CYP2U1 model bound to a POPC membrane. We also performed docking experiments of arachidonic acid (AA) and N-arachidonoylserotonin (AS) in this model. RESULTS: The protein sequence of CYP2U1 displayed two unique characteristics when compared to those of the human CYPs, the presence of a longer N-terminal region upstream of the putative trans-membrane helix (TMH) containing 8 proline residues, and of an insert of about 20 amino acids containing 5 arginine residues between helices A' and A. Its N-terminal part upstream of TMH involved an additional short terminal helix, in a manner similar to what was reported in the crystal structure of Saccharomyces cerevisiae CYP51. Our model also showed a specific interaction between the charged residues of insert AA' and phosphate groups of lipid polar heads, suggesting a possible role of this insert in substrate recruitment. Docking of AA and AS in this model showed these substrates in channel 2ac, with the terminal alkyl chain of AA or the indole ring of AS close to the heme, in agreement with the reported CYP2U1-catalyzed AA and AS hydroxylation regioselectivities. MAJOR CONCLUSION AND GENERAL SIGNIFICANCE: This model should be useful to find new endogenous or exogenous CYP2U1 substrates and to interpret the regioselectivity of their hydroxylation.
    Mots-clés : Access channels, Active site topology, Arachidonic acid, B3S, LSOD, Membrane interaction, molecular dynamics, N-arachidonoylserotonin.

  • N. El Bakkali-Tahéri, S. Tachon, M. Orio, S. Bertaina, M. Martinho, V. Robert, M. Réglier, T. Tron, P. Dorlet, et A. J. Simaan, « Characterization of Cu(II)-reconstituted ACC Oxidase using experimental and theoretical approaches », Archives of Biochemistry and Biophysics, mai 2017.
    Résumé : 1-Aminocyclopropane-1-carboxylic acid oxidase (ACCO) is a non heme iron(II) containing enzyme that catalyzes the final step of the ethylene biosynthesis in plants. The iron(II) ion is bound in a facial triad composed of two histidines and one aspartate (H177, D179 and H234). Several active site variants were generated to provide alternate binding motifs and the enzymes were reconstituted with copper(II). Continuous wave (cw) and pulsed Electron Paramagnetic Resonance (EPR) spectroscopies as well as Density Functional Theory (DFT) calculations were performed and models for the copper(II) binding sites were deduced. In all investigated enzymes, the copper ion is equatorially coordinated by the two histidine residues (H177 and H234) and probably two water molecules. The copper-containing enzymes are inactive, even when hydrogen peroxide is used in peroxide shunt approach. EPR experiments and DFT calculations were undertaken to investigate substrate's (ACC) binding on the copper ion and the results were used to rationalize the lack of copper-mediated activity.
    Mots-clés : ACC Oxidase, B3S, Copper, Density functional theory calculations, Electron paramagnetic resonance, Ethylene, LSOD.

  • J. Keirsse-Haquin, T. Picaud, L. Bordes, A. G. de Gracia, et A. Desbois, « Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study », European biophysics journal: EBJ, sept. 2017.
    Résumé : NADH peroxidase (Npx) and mercuric ion reductase (MerA) are flavoproteins belonging to the pyridine nucleotide:disulfide oxidoreductases (PNDO) and catalyzing the reduction of toxic substrates, i.e., hydrogen peroxide and mercuric ion, respectively. To determine the role of the flavin adenine dinucleotide (FAD) in the detoxification mechanism, the resonance Raman (RR) spectra of these enzymes under various redox and ligation states have been investigated using blue and/or near-UV excitation(s). These data were compared to those previously obtained for glutathione reductase (GR), another enzyme of the PNDO family, but catalyzing the reduction of oxidized glutathione. Spectral differences have been detected for the marker bands of the isoalloxazine ring of Npx, MerA, and GR. They provide evidence for different catalytic mechanisms in these flavoproteins. The RR modes of the oxidized and two-electron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. They also indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center. All these spectroscopic data support an enzyme functioning centered on the Cys-SO(-)/Cys-S(-) redox moiety and a neighbouring His residue. On the contrary, the RR data on various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts.
    Mots-clés : B3S, Detoxification mechanism, Flavin–protein interactions, Isoalloxazine modes, LBMS, LSOD, Resonance Raman.

  • H. Renault, M. De Marothy, G. Jonasson, P. Lara, D. R. Nelson, I. M. Nilsson, F. André, G. von Heijne, et D. Werck-Reichhart, « Gene duplication leads to altered membrane topology of a cytochrome P450 enzyme in seed plants », Molecular Biology and Evolution, mai 2017.
    Résumé : Evolution of the phenolic metabolism was critical for the transition of plants from water to land. A cytochrome P450, CYP73, with cinnamate 4-hydroxylase (C4H) activity, catalyzes the first plant-specific and rate-limiting step in this pathway. The CYP73 gene is absent from green algae, and first detected in bryophytes. A CYP73 duplication occurred in the ancestor of seed plants and was retained in Taxaceae and most angiosperms. In spite of a clear divergence in primary sequence, both paralogs can fulfill comparable cinnamate hydroxylase roles both in vitro and in vivo. One of them seems dedicated to the biosynthesis of lignin precursors. Its N-terminus forms a single membrane spanning helix and its properties and length are highly constrained. The second is characterized by an elongated and variable N-terminus, reminiscent of ancestral CYP73s. Using as proxies the Brachypodium distachyon proteins, we show that the elongation of the N-terminus does not result in an altered subcellular localization, but in a distinct membrane topology. Insertion in the membrane of endoplasmic reticulum via a double-spanning open hairpin structure allows reorientation to the lumen of the catalytic domain of the protein. In agreement with participation to a different functional unit and supramolecular organization, the protein displays altered heme proximal surface. These data suggest the evolution of divergent C4H enzymes feeding different branches of the phenolic network in seed plants. It shows that specialization required for retention of gene duplicates may result from altered protein topology rather than change in enzyme activity.
    Mots-clés : B3S, LSOD.

  • J. Santolini, F. André, S. Jeandroz, et D. Wendehenne, « Nitric oxide synthase in plants: Where do we stand? », Nitric Oxide, vol. 63, p. 30-38, 2017.

  • M. Weisslocker-Schaetzel, F. André, N. Touazi, N. Foresi, M. Lembrouk, P. Dorlet, A. Frelet-Barrand, L. Lamattina, et J. Santolini, « The NOS-like protein from the microalgae Ostreococcus tauri is a genuine and ultrafast NO-producing enzyme », Plant Science: An International Journal of Experimental Plant Biology, vol. 265, p. 100-111, déc. 2017.
    Résumé : The exponential increase of genomes' sequencing has revealed the presence of NO-Synthases (NOS) throughout the tree of life, uncovering an extraordinary diversity of genetic structure and biological functions. Although NO has been shown to be a crucial mediator in plant physiology, NOS sequences seem present solely in green algae genomes, with a first identification in the picoplankton species Ostreococcus tauri. There is no rationale so far to account for the presence of NOS in this early-diverging branch of the green lineage and its absence in land plants. To address the biological function of algae NOS, we cloned, expressed and characterized the NOS oxygenase domain from Ostreococcus tauri (OtNOSoxy). We launched a phylogenetic and structural analysis of algae NOS, and achieved a 3D model of OtNOSoxy by homology modeling. We used a combination of various spectroscopies to characterize the structural and electronic fingerprints of some OtNOSoxy reaction intermediates. The analysis of OtNOSoxy catalytic activity and kinetic efficiency was achieved by stoichiometric stopped-flow. Our results highlight the conserved and particular features of OtNOSoxy structure that might explain its ultrafast NO-producing capacity. This integrative Structure-Catalysis-Function approach could be extended to the whole NOS superfamily and used for predicting potential biological activity for any new NOS.
    Mots-clés : Algae, B3S, Catalysis, Function, LSOD, NO synthase, Plant, Structure.

  • M. Weisslocker-Schaetzel, M. Lembrouk, J. Santolini, et P. Dorlet, « Revisiting the Val/Ile Mutation in Mammalian and Bacterial Nitric Oxide Synthases: A Spectroscopic and Kinetic Study », Biochemistry, vol. 56, nᵒ 5, p. 748-756, févr. 2017.




  • A. Kreimeyer, F. André, C. Gouyette, et T. Huynh-Dinh, « Transmembrane Transport of Adenosine 5'-Triphosphate Using a Lipophilic Cholesteryl Derivative », Angewandte Chemie (International Ed. in English), vol. 37, nᵒ 20, p. 2853-2855, nov. 1998.
    Résumé : The uptake of ATP in liposomes was achieved by using the lipophilic derivative cholesteryloxycarbonyl-ATP (1). Its hydrolysis leading to the release of ATP inside the vesicules (see scheme) was observed with the help of a pH gradient and monitored by 31 P NMR spectroscopy. This is the first successful transfer of a nucleoside 5'-triphosphate across a membrane.
    Mots-clés : B3S, Drug design, Liposomes, LSOD, Membranes, NMR spectroscopy, Nucleotides.
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  1. Bakari, S., André, F., Seigneurin-Berny, D., Delaforge, M., Rolland, N., Frelet-Barrand, A. 2014. Lactococcus lactis, recent developments in functional expression of membrane proteins. In Membrane Proteins Production for Structural Analysis. I. Mus-Veteau, editor. Springer eBook.
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  1. Cabaret, O., Puel, O., Botterel, F., Pean, M., Khoufache, K., Costa, J. M., Delaforge, M., Bretagne, S. (2010). Metabolic detoxication pathways for sterigmatocystin in primary tracheal epithelial cells. Chem Res Toxicol 23,1673-1681.
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  1. Bellanger, A. P., Roussel, A., Millon, L., Delaforge, M., Reboux, G. (2012). Jewelry boxes contaminated by Aspergillus oryzae : an occupational health risk ? J Occup Environ Hyg 9,460-466.
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  9. Hannibal, L., Collins, D., Brassard, J., Chakravarti, R., Vempati, R., Dorlet, P., Santolini, J., Dawson, J. H., Stuehr, D. J. (2012). Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 51,8514-8529.
  10. Hureau, C., Dorlet, P. (2012). Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-b peptides involved in Alzheimer disease. Part 2 : Dependence of Cu(II) binding sites with Ab sequences. Coord. Chem. Rev. 256,2175-2187.
  11. Kwiecien, R. A., Kosieradzka, K., Le Questel, J. Y., Lebreton, J., Fournial, A., Gentil, E., Delaforge, M., Paneth, P., Robins, R. J. (2012). Cytochrome P450 monooxygenase-catalyzed ring opening of the bicyclic amine, nortropine : an experimental and DFT computational study. Chem Cat Chem 4,530-539.
  12. Kwiecien, R. A., Le Questel, J. Y., Lebreton, J., Delaforge, M., Andre, F., Pihan, E., Roussel, A., Fournial, A., Paneth, P., Robins, R. J. (2012). Cytochrome P450-catalyzed degradation of nicotine : fundamental parameters determining hydroxylation by cytochrome P450 2A6 at the 5’-carbon or the N-methyl carbon. J Phys Chem B 116,7827-7840.
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  14. Roussel, S., Reboux, G., Millon, L., Parchas, M. D., Boudih, S., Skana, F., Delaforge, M., Rakotonirainy, M. S. (2012). Microbiological evaluation of ten French archives and link to occupational symptoms. Indoor Air 22,514-522.
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