Hammann P, Parmentier D, Cerciat M, Reimegård J, Helfer A-C, Boisset S, Guillier M, Vandenesch F, Wagner G E H, Romby P, Fechter P
A method to map changes in bacterial surface composition induced by regulatory RNAs in Escherichia coli and Staphylococcus aureus. Journal Article
In: Biochimie, vol. 106, pp. 175–179, 2014, ISSN: 1638-6183 0300-9084, (Place: France).
Abstract | Links | BibTeX | Tags: Bacterial Outer Membrane Proteins/metabolism, Bacterial Proteins/*metabolism, Bacterial/genetics/*metabolism, Base Sequence, Carbocyanines/metabolism, Cell Membrane/*metabolism, Cell Wall/metabolism, Confocal, DIGE, Electrophoresis, Escherichia coli/genetics/*metabolism, Gel, Mass, Matrix-Assisted Laser Desorption-Ionization, Microscopy, Molecular Sequence Data, Non-coding RNAs, Post-transcriptional regulation, PPSE, Reproducibility of Results, RNA, Spectrometry, Staining and Labeling/methods, Staphylococcus aureus/genetics/*metabolism, Surface proteins, Two-Dimensional/methods
@article{hammann_method_2014,
title = {A method to map changes in bacterial surface composition induced by regulatory RNAs in Escherichia coli and Staphylococcus aureus.},
author = {P Hammann and D Parmentier and M Cerciat and J Reimegård and A-C Helfer and S Boisset and M Guillier and F Vandenesch and G E H Wagner and P Romby and P Fechter},
doi = {10.1016/j.biochi.2014.07.011},
issn = {1638-6183 0300-9084},
year = {2014},
date = {2014-01-01},
journal = {Biochimie},
volume = {106},
pages = {175--179},
abstract = {We have adapted a method to map cell surface proteins and to monitor the effect of specific regulatory RNAs on the surface composition of the bacteria. This method involves direct labeling of surface proteins of living bacteria using fluorescent dyes and a subsequent separation of the crude extract by 2D gel electrophoresis. The strategy yields a substantial enrichment in surface proteins over cytoplasmic proteins. We validated this method by monitoring the effect of the regulatory RNA MicA in Escherichia coli, which regulates the synthesis of several outer membrane proteins, and highlighted the role of Staphylococcus aureus RNAIII for the maintenance of cell wall integrity.},
note = {Place: France},
keywords = {Bacterial Outer Membrane Proteins/metabolism, Bacterial Proteins/*metabolism, Bacterial/genetics/*metabolism, Base Sequence, Carbocyanines/metabolism, Cell Membrane/*metabolism, Cell Wall/metabolism, Confocal, DIGE, Electrophoresis, Escherichia coli/genetics/*metabolism, Gel, Mass, Matrix-Assisted Laser Desorption-Ionization, Microscopy, Molecular Sequence Data, Non-coding RNAs, Post-transcriptional regulation, PPSE, Reproducibility of Results, RNA, Spectrometry, Staining and Labeling/methods, Staphylococcus aureus/genetics/*metabolism, Surface proteins, Two-Dimensional/methods},
pubstate = {published},
tppubtype = {article}
}
Schaeffer Evelyne, Dehuyser Laure, Sigwalt David, Flacher Vincent, Bernacchi Serena, Chaloin Olivier, Remy Jean-Serge, Mueller Christopher G, Baati Rachid, Wagner Alain
Dynamic micelles of mannoside glycolipids are more efficient than polymers for inhibiting HIV-1 trans-infection Journal Article
In: Bioconjugate Chemistry, vol. 24, no. 11, pp. 1813–1823, 2013, ISSN: 1520-4812.
Abstract | Links | BibTeX | Tags: Anti-HIV Agents, Calcium, Cells, Chemistry, Cultured, Dendritic Cells, Dose-Response Relationship, Drug, Electron, fluorescence, Glycolipids, HIV, HIV Infections, HIV-1, Human, Humans, immunodeficiency, immunopathology, inhibition, LECTIN, Lectins, lipid, Mannosides, Micelles, Microbial Sensitivity Tests, Microscopy, Models, Molecular, Molecular Structure, Polymers, prophylaxis, Spectrometry, Structure-Activity Relationship, Surface Plasmon Resonance, target, Team-Mueller, Thermodynamics, Transmission, virus
@article{schaeffer_dynamic_2013,
title = {Dynamic micelles of mannoside glycolipids are more efficient than polymers for inhibiting HIV-1 trans-infection},
author = {Evelyne Schaeffer and Laure Dehuyser and David Sigwalt and Vincent Flacher and Serena Bernacchi and Olivier Chaloin and Jean-Serge Remy and Christopher G Mueller and Rachid Baati and Alain Wagner},
doi = {10.1021/bc4000806},
issn = {1520-4812},
year = {2013},
date = {2013-11-01},
journal = {Bioconjugate Chemistry},
volume = {24},
number = {11},
pages = {1813--1823},
abstract = {Mannoside glycolipid conjugates are able to inhibit human immunodeficiency virus type 1 (HIV-1) trans-infection mediated by human dendritic cells (DCs). The conjugates are formed by three building blocks: a linear or branched mannose head, a hydrophilic linker, and a 24-carbon lipid chain. We have shown that, even as single molecules, these compounds efficiently target mannose-binding lectins, such as DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN) important for HIV-1 transmission. With the goal to optimize their inhibitory activity by supramolecular structure formation, we have compared saturated and unsaturated conjugates, as single molecules, self-assemblies of dynamic micelles, and photopolymerized cross-linked polymers. Surface plasmon resonance showed that, unexpectedly, polymers of trivalent conjugates did not display a higher binding affinity for DC-SIGN than single molecules. Interactions on a chip or in solution were independent of calcium; however, binding to DCs was inhibited by a calcium chelator. Moreover, HIV-1 trans-infection was mostly inhibited by dynamic micelles and not by rigid polymers. The inhibition data revealed a clear correlation between the structure and molecular assembly of a conjugate and its biological antiviral activity. We present an interaction model between DC-SIGN and conjugates-either single molecules, micelles, or polymers-that highlights that the most effective interactions by dynamic micelles involve both mannose heads and lipid chains. Our data reveal that trivalent glycolipid conjugates display the highest microbicide potential for HIV prophylaxis, as dynamic micelles conjugates and not as rigid polymers.},
keywords = {Anti-HIV Agents, Calcium, Cells, Chemistry, Cultured, Dendritic Cells, Dose-Response Relationship, Drug, Electron, fluorescence, Glycolipids, HIV, HIV Infections, HIV-1, Human, Humans, immunodeficiency, immunopathology, inhibition, LECTIN, Lectins, lipid, Mannosides, Micelles, Microbial Sensitivity Tests, Microscopy, Models, Molecular, Molecular Structure, Polymers, prophylaxis, Spectrometry, Structure-Activity Relationship, Surface Plasmon Resonance, target, Team-Mueller, Thermodynamics, Transmission, virus},
pubstate = {published},
tppubtype = {article}
}
Hamrita Bechr, Chahed Karim, Trimeche Mounir, Guillier Christelle Lemaitre, Hammann Philippe, Chaïeb Anouar, Korbi Sadok, Chouchane Lotfi
In: Clinica chimica acta; international journal of clinical chemistry, vol. 404, no. 2, pp. 111–118, 2009, ISSN: 1873-3492 0009-8981, (Place: Netherlands).
Abstract | Links | BibTeX | Tags: 80 and over, Adult, Aged, alpha 1-Antitrypsin/*blood, Amino Acid Sequence, Biomarkers, Breast Neoplasms/blood/*pathology, Carcinoma, Ductal/blood/*pathology, Electrophoresis, Female, Gel, Haptoglobins/*analysis, Humans, Mass, Matrix-Assisted Laser Desorption-Ionization, Middle Aged, Molecular Sequence Data, PPSE, Protein Isoforms/blood, proteomics, Spectrometry, Tumor/*blood, Two-Dimensional
@article{hamrita_proteomics-based_2009,
title = {Proteomics-based identification of alpha1-antitrypsin and haptoglobin precursors as novel serum markers in infiltrating ductal breast carcinomas.},
author = {Bechr Hamrita and Karim Chahed and Mounir Trimeche and Christelle Lemaitre Guillier and Philippe Hammann and Anouar Chaïeb and Sadok Korbi and Lotfi Chouchane},
doi = {10.1016/j.cca.2009.03.033},
issn = {1873-3492 0009-8981},
year = {2009},
date = {2009-06-01},
journal = {Clinica chimica acta; international journal of clinical chemistry},
volume = {404},
number = {2},
pages = {111--118},
abstract = {BACKGROUND: The identification of pathological markers of breast cancer for either diagnosis, treatment response or for survival is of critical importance. METHODS: Serum protein profiling using 2-DE separations coupled to matrix-assisted laser desorption ionization mass spectrometry has been used to explore protein alterations in patients with infiltrating ductal breast carcinomas (IDCA). Sera from 39 breast cancer patients and 40 healthy controls were selected for screening study using 2-DE combined with MS. The protein expression patterns obtained after the depletion of high abundance proteins was determined by coomassie blue G-250 stain after 2-DE electrophoresis. RESULTS: Six proteins that expressed differentially in the IDCA group were found. The expression levels of four isoforms corresponding to haptoglobin precursor and two isoforms of alpha1-antitrypsin precursor (alpha1-AT) were upregulated in sera from breast cancer patients. There was an increased expression of both proteins in the sera of patients with various tumor stages (I, II, III) in comparison to healthy women. Applying immunohistochemistry, we further validated alpha1-AT immunoreactivity in 51 formalin-fixed paraffin-embedded sections of breast tumors. Enhanced expression of alpha1-AT like activity has been found in IDCA breast tumors, as well as, in different histological types of breast cancer. No significant association has been found with lymph node occurrence, while in high tumor categories a tendency to an increased expression of alpha1-AT has been found, thereby suggesting a possible role of this protein in tumor growth. CONCLUSIONS: These proteins may constitute new and useful markers of breast cancer that offer a clue to a better understanding of inflammatory pathways and carcinogenesis events linked to breast cancer progression.},
note = {Place: Netherlands},
keywords = {80 and over, Adult, Aged, alpha 1-Antitrypsin/*blood, Amino Acid Sequence, Biomarkers, Breast Neoplasms/blood/*pathology, Carcinoma, Ductal/blood/*pathology, Electrophoresis, Female, Gel, Haptoglobins/*analysis, Humans, Mass, Matrix-Assisted Laser Desorption-Ionization, Middle Aged, Molecular Sequence Data, PPSE, Protein Isoforms/blood, proteomics, Spectrometry, Tumor/*blood, Two-Dimensional},
pubstate = {published},
tppubtype = {article}
}
Bringel Françoise, Hammann Philippe, Kugler Valérie, Arsène-Ploetze Florence
In: Microbiology (Reading, England), vol. 154, no. Pt 9, pp. 2629–2640, 2008, ISSN: 1350-0872 1350-0872, (Place: England).
Abstract | Links | BibTeX | Tags: Arginine/*biosynthesis, Argininosuccinate Lyase/genetics, Bacterial, Bacterial Proteins/*genetics, Bacterial/genetics, Carbon Compounds, Carbon Dioxide/metabolism, Electrophoresis, Gel, Gene Expression Regulation, Genetic, IMP Dehydrogenase/genetics, Inorganic/*metabolism, Lactobacillus plantarum/enzymology/genetics/*metabolism, Mass, Matrix-Assisted Laser Desorption-Ionization, Nucleotides/*biosynthesis, Pentosyltransferases/*genetics, PPSE, proteomics, Repressor Proteins/*genetics, Reverse Transcriptase Polymerase Chain Reaction, RNA, Spectrometry, Transcription, Two-Dimensional
@article{bringel_lactobacillus_2008,
title = {Lactobacillus plantarum response to inorganic carbon concentrations: PyrR2-dependent and -independent transcription regulation of genes involved in arginine and nucleotide metabolism.},
author = {Françoise Bringel and Philippe Hammann and Valérie Kugler and Florence Arsène-Ploetze},
doi = {10.1099/mic.0.2008/018184-0},
issn = {1350-0872 1350-0872},
year = {2008},
date = {2008-09-01},
journal = {Microbiology (Reading, England)},
volume = {154},
number = {Pt 9},
pages = {2629--2640},
abstract = {Lactobacillus plantarum susbp. plantarum is a capnophilic Gram-positive heterotroph with optimal growth in 4 % CO(2)-enriched air. At low inorganic carbon (C(i)) concentrations, the pyr genes encoding the enzymes of the pyrimidine biosynthetic pathway were overexpressed, in agreement with a previous study showing that these genes are regulated at the transcription level in response to C(i) via a PyrR(2)-mediated mechanism. A previous study of high-CO(2)-requiring (HCR) mutants revealed an unknown genetic link between arginine regulation and C(i)-dependent nutritional needs. To better understand L. plantarum's adaptation to C(i) availability, additional C(i)-responsive genes were sought in the arginine biosynthetic pathway (arg and car genes) using slot-blot hybridization and a proteomic differential 2D gel electrophoresis (DIGE) global approach. Besides the nine pyr-encoded proteins, 16 new Icr (inorganic-carbon-regulated) proteins accumulated differentially in response to C(i) availability, suggesting that the C(i) response involves several metabolic pathways and adaptation processes. Among these Icr proteins only argininosuccinate lyase, encoded by argH, was involved in arginine biosynthesis. Three proteins involved in the purine biosynthetic pathway and nucleotide conversion, adenylate kinase (Adk), GMP synthase (GuaA), and IMP dehydrogenase (GuaB), accumulated differentially in response to changes in C(i) levels. Expression of the Icr protein-encoding genes argH and guaB was regulated at the transcription level or by RNA stability in response to C(i) availability, as previously demonstrated for the pyr genes. However, PyrR(2) was not essential for the C(i)-regulated transcription of argH and guaB, demonstrating that PyrR(2) modulates only a subset of C(i)-regulated genes. These results suggest that the C(i) response may involve at least two regulatory mechanisms in L. plantarum.},
note = {Place: England},
keywords = {Arginine/*biosynthesis, Argininosuccinate Lyase/genetics, Bacterial, Bacterial Proteins/*genetics, Bacterial/genetics, Carbon Compounds, Carbon Dioxide/metabolism, Electrophoresis, Gel, Gene Expression Regulation, Genetic, IMP Dehydrogenase/genetics, Inorganic/*metabolism, Lactobacillus plantarum/enzymology/genetics/*metabolism, Mass, Matrix-Assisted Laser Desorption-Ionization, Nucleotides/*biosynthesis, Pentosyltransferases/*genetics, PPSE, proteomics, Repressor Proteins/*genetics, Reverse Transcriptase Polymerase Chain Reaction, RNA, Spectrometry, Transcription, Two-Dimensional},
pubstate = {published},
tppubtype = {article}
}
Przykorska A., Solecka K., Olszak K., Keith G., Nawrot B., Kuligowska E.
Wheat (Triticum vulgare) chloroplast nuclease ChSI exhibits 5' flap structure-specific endonuclease activity Journal Article
In: Biochemistry, vol. 43, no. 35, pp. 11283-94, 2004, (0006-2960 Journal Article).
Abstract | BibTeX | Tags: &, Acid, Catalysis, Chloroplasts/*enzymology, Conformation, Desorption-Ionization, DNA, Endonucleases/*chemistry/isolation, Exonucleases/chemistry/metabolism, Flap, Gov't, Hydrolysis, KEITH, Kinetics, Laser, Mass, Matrix-Assisted, Non-U.S., Nucleic, Oligonucleotides/chemical, Plant/chemistry/metabolism, purification/*metabolism, Relationship, Single-Stranded/chemistry/metabolism, Specificity, Spectrometry, Structure-Activity, Substrate, Support, synthesis/metabolism, Thermodynamics, Triticum/*enzymology
@article{,
title = {Wheat (Triticum vulgare) chloroplast nuclease ChSI exhibits 5' flap structure-specific endonuclease activity},
author = { A. Przykorska and K. Solecka and K. Olszak and G. Keith and B. Nawrot and E. Kuligowska},
year = {2004},
date = {2004-01-01},
journal = {Biochemistry},
volume = {43},
number = {35},
pages = {11283-94},
abstract = {The structure-specific ChSI nuclease from wheat (Triticum vulgare) chloroplast stroma has been previously purified and characterized in our laboratory. It is a single-strand-specific DNA and RNA endonuclease. Although the enzyme has been initially characterized and used as a structural probe, its biological function is still unknown. Localization of the ChSI enzyme inside chloroplasts, possessing their own DNA that is generally highly exposed to UV light and often affected by numerous redox reactions and electron transfer processes, might suggest, however, that this enzyme could be involved in DNA repair. The repair of some types of DNA damage has been shown to proceed through branched DNA intermediates which are substrates for the structure-specific DNA endonucleases. Thus we tested the substrate specificity of ChSI endonuclease toward various branched DNAs containing 5' flap, 5' pseudoflap, 3' pseudoflap, or single-stranded bulged structural motifs. It appears that ChSI has a high 5' flap structure-specific endonucleolytic activity. The catalytic efficiency (k(cat)/K(M)) of the enzyme is significantly higher for the 5' flap substrate than for single-stranded DNA. The ChSI 5' flap activity was inhibited by high concentrations of Mg(2+), Mn(2+), Zn(2+), or Ca(2+). However, low concentrations of divalent cations could restore the loss of ChSI activity as a consequence of EDTA pretreatment. In contrast to other known 5' flap nucleases, the chloroplast enzyme ChSI does not possess any 5'-->3' exonuclease activity on double-stranded DNA. Therefore, we conclude that ChSI is a 5' flap structure-specific endonuclease with nucleolytic activity toward single-stranded substrates.},
note = {0006-2960
Journal Article},
keywords = {&, Acid, Catalysis, Chloroplasts/*enzymology, Conformation, Desorption-Ionization, DNA, Endonucleases/*chemistry/isolation, Exonucleases/chemistry/metabolism, Flap, Gov't, Hydrolysis, KEITH, Kinetics, Laser, Mass, Matrix-Assisted, Non-U.S., Nucleic, Oligonucleotides/chemical, Plant/chemistry/metabolism, purification/*metabolism, Relationship, Single-Stranded/chemistry/metabolism, Specificity, Spectrometry, Structure-Activity, Substrate, Support, synthesis/metabolism, Thermodynamics, Triticum/*enzymology},
pubstate = {published},
tppubtype = {article}
}
Thouzeau Cécile, Maho Yvon Le, Froget Guillaume, Sabatier Laurence, Bohec Céline Le, Hoffmann Jules A, Bulet Philippe
Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus Journal Article
In: J. Biol. Chem., vol. 278, no. 51, pp. 51053–51058, 2003, ISSN: 0021-9258.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry
@article{thouzeau_spheniscins_2003,
title = {Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus},
author = {Cécile Thouzeau and Yvon Le Maho and Guillaume Froget and Laurence Sabatier and Céline Le Bohec and Jules A Hoffmann and Philippe Bulet},
doi = {10.1074/jbc.M306839200},
issn = {0021-9258},
year = {2003},
date = {2003-12-01},
journal = {J. Biol. Chem.},
volume = {278},
number = {51},
pages = {51053--51058},
abstract = {During the last part of egg incubation in king penguins, the male can preserve undigested food in the stomach for several weeks. This ensures survival of the newly hatched chick, in cases where the return of the foraging female from the sea is delayed. In accordance with the characterization of stress-induced bacteria, we demonstrate the occurrence of strong antimicrobial activities in preserved stomach contents. We isolated and fully characterized two isoforms of a novel 38-residue antimicrobial peptide (AMP), spheniscin, belonging to the beta-defensin subfamily. Spheniscin concentration was found to strongly increase during the period of food storage. Using a synthetic version of one of two spheniscin isoforms, we established that this peptide has a broad activity spectrum, affecting the growth of both pathogenic bacteria and fungi. Altogether, our data suggest that spheniscins and other, not yet identified, antimicrobial substances may play a role in the long term preservation of stored food in the stomach of king penguins.},
keywords = {Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Sabatier Laurence, Jouanguy Emmanuelle, Dostert Catherine, Zachary Daniel, Dimarcq Jean-Luc, Bulet Philippe, Imler Jean-Luc
Pherokine-2 and -3 Journal Article
In: European journal of biochemistry / FEBS, vol. 270, no. 16, pp. 3398–3407, 2003, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Antibody Formation, Base Sequence, Hemolymph, imler, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrometry
@article{sabatier_pherokine-2_2003,
title = {Pherokine-2 and -3},
author = {Laurence Sabatier and Emmanuelle Jouanguy and Catherine Dostert and Daniel Zachary and Jean-Luc Dimarcq and Philippe Bulet and Jean-Luc Imler},
issn = {0014-2956},
year = {2003},
date = {2003-01-01},
journal = {European journal of biochemistry / FEBS},
volume = {270},
number = {16},
pages = {3398--3407},
abstract = {Drosophila is a powerful model system to study the regulatory and effector mechanisms of innate immunity. To identify molecules induced in the course of viral infection in this insect, we have developed a model based on intrathoracic injection of the picorna-like Drosophila C virus (DCV). We have used MALDI-TOF mass spectrometry to compare the hemolymph of DCV infected flies and control flies. By contrast with the strong humoral response triggered by injection of bacteria or fungal spores, we have identified only one molecule induced in the hemolymph of virus infected flies. This molecule, pherokine-2 (Phk-2), is related to OS-D/A10 (Phk-1), which was previously characterized as a putative odor/pheromone binding protein specifically expressed in antennae. The virus-induced molecule is also similar to the product of the gene CG9358 (Phk-3), which is induced by septic injury. Both Phk-2 and Phk-3 are strongly expressed during metamorphosis, suggesting that they may participate in tissue-remodeling.},
keywords = {Animals, Antibody Formation, Base Sequence, Hemolymph, imler, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Bianco Alberto, Pellarini Federica, Tossi Alessandro, Giangaspero Anna, Zelezetsky Igor, Briand Jean-Paul, Prato Maurizio
Solid-phase synthesis of fullerene-peptides Journal Article
In: Journal of the American Chemical Society, vol. 124, no. 42, pp. 12543–12549, 2002, ISSN: 0002-7863.
Abstract | Links | BibTeX | Tags: Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco
@article{pantarotto_solid-phase_2002,
title = {Solid-phase synthesis of fullerene-peptides},
author = {Davide Pantarotto and Alberto Bianco and Federica Pellarini and Alessandro Tossi and Anna Giangaspero and Igor Zelezetsky and Jean-Paul Briand and Maurizio Prato},
doi = {10.1021/ja027603q},
issn = {0002-7863},
year = {2002},
date = {2002-10-01},
journal = {Journal of the American Chemical Society},
volume = {124},
number = {42},
pages = {12543--12549},
abstract = {The solid-phase synthesis of peptides (SPPS) containing [60]fullerene-functionalized amino acids is reported. A new amino acid, fulleropyrrolidino-glutamic acid (Fgu), is used for the SPPS of a series of analogues of different length based on the natural Leu(5)-Enkephalin and on cationic antimicrobial peptides. These fullero-peptides were prepared on different solid supports to analyze the influence of the resin on the synthesis. Optimized protocols for the coupling and deprotection procedures were determined allowing the synthesis of highly pure peptides in sufficient quantities for evaluation of biological activities. In particular, to avoid side reactions of the fullerene moiety with bases and nucleophiles, the removal of the protecting groups was performed under inert conditions (nitrogen or argon in the dark). We have encountered serious problems with the recovery of the crude compounds, especially when Fgu was inserted in the proximity of the resin core as fullero-peptides tend to remain embedded inside the resin. Eventually, all of the fullero-peptides were easily purified, and the cationic peptides were tested for their antimicrobial activities. They displayed a specific activity against the Gram-positive bacterium S. aureus and also lysed erythrocytes. The availability of a fullero-amino acid easily useable in the SPPS of fullero-peptides may thus open the way to the synthesis of new types of biologically active oligomers.},
keywords = {Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Ligoxygakis Petros, Bulet Philippe, Reichhart Jean-Marc
Critical evaluation of the role of the Toll-like receptor 18-Wheeler in the host defense of Drosophila Journal Article
In: EMBO Rep., vol. 3, no. 7, pp. 666–673, 2002, ISSN: 1469-221X.
Abstract | Links | BibTeX | Tags: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Cell Adhesion Molecules, Fat Body, Gene Expression Regulation, Genes, Immunohistochemistry, Immunologic, Insect, Insect Proteins, Larva, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Membrane Proteins, Receptors, reichhart, Reporter, Spectrometry, Transgenes
@article{ligoxygakis_critical_2002,
title = {Critical evaluation of the role of the Toll-like receptor 18-Wheeler in the host defense of Drosophila},
author = {Petros Ligoxygakis and Philippe Bulet and Jean-Marc Reichhart},
doi = {10.1093/embo-reports/kvf130},
issn = {1469-221X},
year = {2002},
date = {2002-01-01},
journal = {EMBO Rep.},
volume = {3},
number = {7},
pages = {666--673},
abstract = {Essential aspects of innate immune responses to microbial infections appear to be conserved between insects and mammals. In particular, in both groups, transmembrane receptors of the Toll superfamily play a crucial role in activating immune defenses. The Drosophila Toll family member 18-Wheeler had been proposed to sense Gram-negative infection and direct selective expression of peptides active against Gram-negative bacteria. Here we re-examine the role of 18-Wheeler and show that in adults it is dispensable for immune responses. In larvae, 18wheeler is required for normal fat body development, and in mutant larvae induction of all antimicrobial peptide genes, and not only of those directed against Gram-negative bacteria, is compromised. 18-Wheeler does not qualify as a pattern recognition receptor of Gram-negative bacteria.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Cell Adhesion Molecules, Fat Body, Gene Expression Regulation, Genes, Immunohistochemistry, Immunologic, Insect, Insect Proteins, Larva, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Membrane Proteins, Receptors, reichhart, Reporter, Spectrometry, Transgenes},
pubstate = {published},
tppubtype = {article}
}
Uttenweiler-Joseph S, Moniatte M, Lagueux Marie, Dorsselaer Van A, Hoffmann Jules A, Bulet Philippe
Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study Journal Article
In: Proc. Natl. Acad. Sci. U.S.A., vol. 95, no. 19, pp. 11342–11347, 1998, ISSN: 0027-8424.
Abstract | BibTeX | Tags: Animals, bacteria, Chromatography, Cloning, Hemolymph, High Pressure Liquid, hoffmann, Immunity, Insect Proteins, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, messenger, Molecular, Peptides, Protein Precursors, RNA, Sequence Analysis, Spectrometry, Time Factors
@article{uttenweiler-joseph_differential_1998,
title = {Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study},
author = {S Uttenweiler-Joseph and M Moniatte and Marie Lagueux and Van A Dorsselaer and Jules A Hoffmann and Philippe Bulet},
issn = {0027-8424},
year = {1998},
date = {1998-09-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {95},
number = {19},
pages = {11342--11347},
abstract = {We have developed an approach based on a differential mass spectrometric analysis to detect molecules induced during the immune response of Drosophila, regardless of their biological activities. For this, we have applied directly matrix-assisted laser desorption/ionization MS to hemolymph samples from individual flies before and after an immune challenge. This method provided precise information on the molecular masses of immune-induced molecules and allowed the detection, in the molecular range of 1.5-11 kDa, of 24 Drosophila immune-induced molecules (DIMs). These molecules are all peptides, and four correspond to already characterized antimicrobial peptides. We have further analyzed the induction of the various peptides by immune challenge in wild-type flies and in mutants with a compromised antimicrobial response. We also describe a methodology combining matrix-assisted laser desorption ionization time-of-flight MS, HPLC, and Edman degradation, which yielded the peptide sequence of three of the DIMs. Finally, molecular cloning and Northern blot analyses revealed that one of the DIMs is produced as a prepropeptide and is inducible on a bacterial challenge.},
keywords = {Animals, bacteria, Chromatography, Cloning, Hemolymph, High Pressure Liquid, hoffmann, Immunity, Insect Proteins, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, messenger, Molecular, Peptides, Protein Precursors, RNA, Sequence Analysis, Spectrometry, Time Factors},
pubstate = {published},
tppubtype = {article}
}
Bulet Philippe, Uttenweiler-Joseph S, Moniatte M, Dorsselaer Van A, Hoffmann Jules A
Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study Journal Article
In: J. Protein Chem., vol. 17, no. 6, pp. 528–529, 1998, ISSN: 0277-8033.
BibTeX | Tags: Animals, Anti-Infective Agents, hoffmann, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Peptide Biosynthesis, Peptides, Spectrometry
@article{bulet_differential_1998,
title = {Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study},
author = {Philippe Bulet and S Uttenweiler-Joseph and M Moniatte and Van A Dorsselaer and Jules A Hoffmann},
issn = {0277-8033},
year = {1998},
date = {1998-08-01},
journal = {J. Protein Chem.},
volume = {17},
number = {6},
pages = {528--529},
keywords = {Animals, Anti-Infective Agents, hoffmann, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Peptide Biosynthesis, Peptides, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Taguchi S, Bulet Philippe, Hoffmann Jules A
A novel insect defensin from the ant Formica rufa Journal Article
In: Biochimie, vol. 80, no. 4, pp. 343–346, 1998, ISSN: 0300-9084.
Abstract | BibTeX | Tags: Amino Acid, Animals, Anti-Bacterial Agents, Ants, Chromatography, High Pressure Liquid, hoffmann, Insect Proteins, insects, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Structure, Secondary, Sequence Alignment, Sequence Homology, Spectrometry
@article{taguchi_novel_1998,
title = {A novel insect defensin from the ant Formica rufa},
author = {S Taguchi and Philippe Bulet and Jules A Hoffmann},
issn = {0300-9084},
year = {1998},
date = {1998-04-01},
journal = {Biochimie},
volume = {80},
number = {4},
pages = {343--346},
abstract = {By combination of size exclusion and reversed-phase chromatography, we have isolated a novel member of insect defensin-type antimicrobial peptides from the entire bodies of bacteria-challenged Formica rufa (hymenoptera, formicidae). The molecular mass of the purified peptide was estimated to be 4120.42 by matrix-assisted laser desorption/ionization-time of flight/mass spectrometry. Sequence analysis revealed that this peptide consisted of 40 amino acid residues with six cysteines engaged in the formation of three intramolecular disulfide bridges. This peptide is unique among the arthropod defensins in terms of the presence of asparatic acid and alanine at position 33 and as C-terminal residue, respectively. In addition, this novel defensin from Formica rufa has the particularity to have no C-terminal extension in contrast to those reported for other hymenoptera defensins.},
keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Ants, Chromatography, High Pressure Liquid, hoffmann, Insect Proteins, insects, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Structure, Secondary, Sequence Alignment, Sequence Homology, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Rosenthal G A, Reichhart Jean-Marc, Hoffmann Jules A
L-canavanine incorporation into vitellogenin and macromolecular conformation Journal Article
In: J. Biol. Chem., vol. 264, no. 23, pp. 13693–13696, 1989, ISSN: 0021-9258.
Abstract | BibTeX | Tags: Animals, Antibodies, Canavanine, fluorescence, Grasshoppers, hoffmann, M3i, Monoclonal, Protein Conformation, reichhart, Spectrometry, Vitellogenins
@article{rosenthal_l-canavanine_1989,
title = {L-canavanine incorporation into vitellogenin and macromolecular conformation},
author = {G A Rosenthal and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0021-9258},
year = {1989},
date = {1989-01-01},
journal = {J. Biol. Chem.},
volume = {264},
number = {23},
pages = {13693--13696},
abstract = {L-Canavanine is a potentially deleterious arginine antimetabolite whose toxicity is expressed in canavanine-sensitive organisms ranging from viruses to humans. Canavanine, a substrate for arginyl-tRNA synthetase, is incorporated into nascent polypeptide chains in place of arginine. This substitution results in the production of structurally aberrant, canavanyl proteins. Chemical, physical, and immunological studies of native and canavanine-containing vitellogenin obtained from female migratory locusts (Locusta migratoria migratorioides (Orthoptera] provide the first experimental evidence that canavanine can disrupt the tertiary and/or quaternary structure that yields the three-dimensional conformation unique to the protein. These findings enhance our understanding of the biochemical basis for canavanine's antimetabolic and potent insecticidal properties.},
keywords = {Animals, Antibodies, Canavanine, fluorescence, Grasshoppers, hoffmann, M3i, Monoclonal, Protein Conformation, reichhart, Spectrometry, Vitellogenins},
pubstate = {published},
tppubtype = {article}
}