{"title":"A novel mechanism of antibiotic resistance: study of the complex state of peptides with bacterial Staphylococcus aureus ribosomes","authors":"Laurent Verdier , Josyane Gharbi-Benarous , Gildas Bertho , Pascale Mauvais , Jean-Pierre Girault","doi":"10.1016/S1387-1609(01)01316-0","DOIUrl":"10.1016/S1387-1609(01)01316-0","url":null,"abstract":"<div><p>Two antibiotic resistance peptides, the E-peptide (MRLFV) and the K-peptide (MRFFV) conferring macrolide and ketolide resistance, respectively, were studied in the complex state with bacterial <em>Staphylococcus aureus</em> ribosomes after a conformational analysis by NMR spectroscopy and molecular modeling of the unbound molecules. <em>T</em>2 (CPMG) measurements were used to characterize equilibrium binding of antibiotic resistance peptides to bacterial ribosomes. Additionally, interactions of antibiotic resistance peptide to ribosomes were investigated using two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY), resulting in bound structures compatible with the experimental NMR data.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 745-750"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01316-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81612448","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Christine Hemmerlin , Angélique Phan Chan Du , Zouhair Elhilali , Avrilia Moulia , Vassilios Tsikaris , Maria Sakarellos-Daitsiotis , Constantinos Sakarellos , Eleni Dotsika , Athanasios G Tzioufas , Haralampos M Moutsopoulos , Manh-Thong Cung
{"title":"Conformational study of the complementary peptide to a B-cell epitope of the La/SSB autoantigen","authors":"Christine Hemmerlin , Angélique Phan Chan Du , Zouhair Elhilali , Avrilia Moulia , Vassilios Tsikaris , Maria Sakarellos-Daitsiotis , Constantinos Sakarellos , Eleni Dotsika , Athanasios G Tzioufas , Haralampos M Moutsopoulos , Manh-Thong Cung","doi":"10.1016/S1387-1609(01)01296-8","DOIUrl":"10.1016/S1387-1609(01)01296-8","url":null,"abstract":"<div><p>Starting from the 20-mer peptide 289–308, one of the experimentally characterized B-cell epitopes of the La/SSB autoantigen, the complementary peptide cpl(289–308), encoded by the complementary RNA was designed. The conformational properties of the cpl(289–308) were investigated in DMSO solution with the combined use of NMR data (vicinal coupling constants, NOE effects and temperature coefficient values), molecular modelling calculations of energy minimization and molecular dynamics. MD calculations led to a folded structure in which a βI-turn, stabilized by the H<sub>8</sub> amide proton to the F<sub>5</sub> carbonyl hydrogen bond, was found for the F<sub>5</sub>P<sub>6</sub>S<sub>7</sub>H<sub>8</sub> sequence, whereas two γ-turns, centred around the E<sub>15</sub> and I<sub>18</sub> residues respectively, were found in the C-terminal part of the peptide. In the whole crown folded structure of the peptide, the Y<sub>4</sub>, F<sub>5</sub>, H<sub>8</sub>, F<sub>9</sub> and F<sub>10</sub> aromatic side chains are situated on one side with the E<sub>13</sub>, E<sub>15</sub>, T<sub>17</sub> and C<sub>20</sub> side chains on the other. This 3D structure resembles and could mimic the binding site of an antibody.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 729-733"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01296-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75697691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Conformational analysis by NMR and molecular modelling of the 41–62 hydrophilic region of HIV-1 encoded virus protein U (Vpu). Effect of the phosphorylation on sites 52 and 56","authors":"Gaël Coadou , Nathalie Évrard-Todeschi , Josyane Gharbi-Benarous , Richard Benarous , Jean-Pierre Girault","doi":"10.1016/S1387-1609(01)01320-2","DOIUrl":"10.1016/S1387-1609(01)01320-2","url":null,"abstract":"<div><p>The peptide of 22 amino acid residues, Vpu_P<sup>41–62</sup>, phosphorylated at the two sites Ser<sup>52</sup> and Ser<sup>56</sup> has been implicated in the degradation of CD4 receptor molecules, an important stage of the pathways to human immunodeficiency virus type 1 pathology (HIV-1). In order to assess the structural influence of phosphorylation, a conformational analysis by NMR and molecular simulation have been carried out for the phosphorylated Vpu_P<sup>41–62</sup>, and non-phosphorylated Vpu<sup>41–62</sup> in both H<sub>2</sub>O (at pH 3.5 and 7.2) and a 1:1 mixture of H<sub>2</sub>O and trifluoroethanol. Analysis of the short-, medium-range NOE connectivities and of the secondary chemical shifts indicated that the peptide segment (42–49) shows a less well-defined helix propensity. The 50–62 segment forms a loop with the phosphate group pointing away, a short β-strand and a flexible extended ‘tail’ of residues 60–62. Differences in this molecular region 50-62 suggest that conformational changes of Vpu_P, play a potential role in Vpu_P-induced degradation of CD4 molecules.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 751-758"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01320-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73718321","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Emeric Wasielewski , Mohamed A. Abdallah , Pavel Kyslik , Bruno Kieffer
{"title":"Sequence determination and resonance assignments of an Azomonas siderophore using 13C natural abundance 13C–1H HNCA experiment","authors":"Emeric Wasielewski , Mohamed A. Abdallah , Pavel Kyslik , Bruno Kieffer","doi":"10.1016/S1387-1609(01)01294-4","DOIUrl":"10.1016/S1387-1609(01)01294-4","url":null,"abstract":"<div><p>The determination of the amino acid sequence of small peptides as siderophores is commonly performed using long-range HMBC correlation experiments. However, this type of experiment can lead to ambiguities in the assignment resulting in erroneous primary sequence determination. In this paper, we propose to use an HNCA type experiment on a <sup>15</sup>N-labelled sample in order to avoid these ambiguities. This experiment was successfully used to determine the primary sequence of azoverdin, a siderophore produced by <em>Azomonas</em>.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 765-770"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01294-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90702400","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"IRM et SRM 1H-1D in vivo à 7 T d’un modèle de régénération musculaire sur la souris","authors":"Catherine Sébrié, Brigitte Gillet, Jean-Claude Belœil","doi":"10.1016/S1387-1609(01)01324-X","DOIUrl":"10.1016/S1387-1609(01)01324-X","url":null,"abstract":"<div><p>In this study, skeletal muscle degeneration–regeneration, induced by notexin (a myotoxic substance) injection is studied by Magnetic Resonance Imaging (MRI) and by histological cuts (hematoxylin/eosin and Evans blue colorations). Comparison between MR images and histological cuts results (necrosis, myoblasts replication and fusion) permits MR images interpretation. From day 0 to day 13 after notexin injection, injected zone images are very different from those realized in healthy muscles. Preliminary localized 1D <sup>1</sup>H-MRS (Magnetic Resonance Spectroscopy) study is also reported.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 783-787"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01324-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82847968","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Recent developments in the characterization of water interacting with proteins by 17O NMR","authors":"Sandrine Besnard, Évelyne Baguet","doi":"10.1016/S1387-1609(01)01293-2","DOIUrl":"10.1016/S1387-1609(01)01293-2","url":null,"abstract":"<div><p>Transverse and longitudinal <sup>17</sup>O-water relaxation rates were detected in different samples of BSA solutions after one-quantum and triple-quantum-filtered NMR sequences. Another contribution other than quadrupolar relaxation was found for transverse relaxation, which did not change significantly with the concentration and hence could not correspond to agglomeration of proteins. This was interpreted as chemical exchange between different types of <sup>17</sup>O-water in fast motion; probably free water and water weakly bound to the proteins. At lower BSA concentrations, two peaks were detected for water; this was in agreement with this hypothesis. The interactions between BSA and lactic acid were also studied. It was shown that at a sufficient concentration of lactic acid, the number of strongly bound water molecules detected diminishes. On the other hand, the weakly bound water properties do not change significantly.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 771-774"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01293-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82263669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Expression and purification of threonyl tRNA synthetase RNA binding domain for heteronuclear NMR studies","authors":"Sophie Raibaud, Noémi Fukuhara , Frédéric Dardel","doi":"10.1016/S1387-1609(01)01295-6","DOIUrl":"10.1016/S1387-1609(01)01295-6","url":null,"abstract":"<div><p>Heteronuclear NMR is a straightforward technique for the analysis of contact areas between one protein and its substrates. We have chosen this approach to study the interaction of threonyl-tRNA synthetase (ThrRS) with its two substrates. ThrRS forms a complex with the anticodon loop of <sup>Thr</sup>tRNA and also with a part of its mRNA, the second interaction being involved in the regulation of ThrRS expression. In these two cases, the interacting part of ThrRS is mostly limited to its C-terminal domain. A two-step study has been conducted: using a first genetic construction, we have validated our approach, which was then modified to improve the solubility and the stability of the recombinant domain. The latter construct was used to prepare an 15N labelled sample which gave heteronuclear NMR spectra of sufficient quality for structure and interaction studies.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 725-728"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01295-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89834394","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ophélie Fliniaux , François Mesnard , Sophie Raynaud , Sylvie Baltora , Richard J Robins , Marc-André Fliniaux
{"title":"Use of heteronuclear multiple bond coherence NMR spectroscopy to monitor nitrogen metabolism in a transformed root culture of Datura stramonium","authors":"Ophélie Fliniaux , François Mesnard , Sophie Raynaud , Sylvie Baltora , Richard J Robins , Marc-André Fliniaux","doi":"10.1016/S1387-1609(01)01318-4","DOIUrl":"10.1016/S1387-1609(01)01318-4","url":null,"abstract":"<div><p>In order to examine the factors that regulate the flux of primary metabolites into tropane alkaloids, Nuclear Magnetic Resonance spectroscopy (NMR) has been used to monitor nitrogen metabolism in transformed root cultures of <em>Datura stramonium</em> fed with (<sup>15</sup>NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub> and K<sup>15</sup>NO<sub>3</sub>. This study employs the technique of Heteronuclear Multiple Bond Coherence (HMBC) NMR spectroscopy, which combines the advantages of both bidimensional resolution and <sup>1</sup>H NMR sensitivity. Moreover, the HMBC sequence allows the <sup>15</sup>N bound to labile protons to be observed via <sup>2</sup><em>J</em> and/or <sup>3</sup><em>J</em> couplings, which is very appropriate for the observation of tropane alkaloids. In transformed roots of <em>Datura stramonium</em>, in addition to the amino acids normally observed in monodimensional <sup>15</sup>N NMR, other amino acids are resolved by HMBC. Labelled peaks due to <em>N</em>-acetyl compounds and to uridine are identified. While these primary metabolites were also seen in cell cultures of <em>Nicotiana plumbaginifolia</em>, cross peaks corresponding to secondary metabolites, such as tropine, were also observed. This is the first time that such secondary products have been found by this technique.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 775-778"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01318-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84327973","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nicolas Mandard , Henri Labbé , Pedro Da Silva , Charles Hetru , Céline Landon , Françoise Vovelle
{"title":"Rôle des ponts disulfure dans le repliement en épingle à cheveux de l’androctonine. Relations structure–activité","authors":"Nicolas Mandard , Henri Labbé , Pedro Da Silva , Charles Hetru , Céline Landon , Françoise Vovelle","doi":"10.1016/S1387-1609(01)01297-X","DOIUrl":"10.1016/S1387-1609(01)01297-X","url":null,"abstract":"<div><p>Androctonin is a 25-residue antibacterial peptide extracted from the hemolymph of the scorpion <em>Androctonus australis.</em> In order to understand the structural requirements for hairpin fold and for interactions with the bacterial membrane, we have analysed the chemical shifts and the nOes of three synthetic androctonin mutants for which the disulfide bridges were selectively removed.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 735-738"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01297-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75589840","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Arlette Trokiner présidente du GERM, Arlette Trokiner president of GERM
{"title":"Avant-propos","authors":"Arlette Trokiner présidente du GERM, Arlette Trokiner president of GERM","doi":"10.1016/S1387-1609(01)01335-4","DOIUrl":"https://doi.org/10.1016/S1387-1609(01)01335-4","url":null,"abstract":"","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Page 723"},"PeriodicalIF":0.0,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01335-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91673740","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}