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1. IFNγ causes mitochondrial dysfunction and oxidative stress in myositis

Author: Catalina Abad, Iago Pinal-Fernandez, Clement Guillou, Gwladys Bourdenet, Laurent Drouot, Pascal Cosette, Margherita Giannini, Lea Debrut, Laetitia Jean, Sophie Bernard, Damien Genty, Rachid Zoubairi, Isabelle Remy-Jouet, Bernard Geny, Christian Boitard, Andrew Mammen, Alain Meyer, and Olivier Boyer
Subjects: Science
Abstract: Abstract Idiopathic inflammatory myopathies (IIMs) are severe autoimmune diseases with poorly understood pathogenesis and unmet medical needs. Here, we examine the role of interferon γ (IFNγ) using NOD female mice deficient in the inducible T cell co-stimulator (Icos), which have previously been shown to develop spontaneous IFNγ-driven myositis mimicking human disease. Using muscle proteomic and spatial transcriptomic analyses we reveal profound myofiber metabolic dysregulation in these mice. In addition, we report muscle mitochondrial abnormalities and oxidative stress in diseased mice. Supporting a pathogenic role for oxidative stress, treatment with a reactive oxygen species (ROS) buffer compound alleviated myositis, preserved muscle mitochondrial ultrastructure and respiration, and reduced inflammation. Mitochondrial anomalies and oxidative stress were diminished following anti-IFNγ treatment. Further transcriptomic analysis in IIMs patients and human myoblast in vitro studies supported the link between IFNγ and mitochondrial dysfunction observed in mice. These results suggest that mitochondrial dysfunction, ROS and inflammation are interconnected in a self-maintenance loop, opening perspectives for mitochondria therapy and/or ROS targeting drugs in myositis.
Published: 2024
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2. Gingival proteomics reveals the role of TGF beta and YAP/TAZ signaling in Raine syndrome fibrosis

Author: Cláudio Rodrigues Rezende Costa, Rym Chalgoumi, Amina Baker, Clément Guillou, Paulo Marcio Yamaguti, Victor Simancas Escorcia, Lilia Abbad, Bruna Rabelo Amorin, Caroline Lourenço de Lima, Vidjea Cannaya, Mourad Benassarou, Ariane Berdal, Christos Chatziantoniou, Olivier Cases, Pascal Cosette, Renata Kozyraki, and Ana Carolina Acevedo
Subjects: FAM20C, FAM20A, Secretome, Proteome, Raine syndrome, TGF beta, Medicine, Science
Abstract: Abstract Raine syndrome (RNS) is a rare autosomal recessive osteosclerotic dysplasia. RNS is caused by loss-of-function disease-causative variants of the FAM20C gene that encodes a kinase that phosphorylates most of the secreted proteins found in the body fluids and extracellular matrix. The most common RNS clinical features are generalized osteosclerosis, facial dysmorphism, intracerebral calcifications and respiratory defects. In non-lethal RNS forms, oral traits include a well-studied hypoplastic amelogenesis imperfecta (AI) and a much less characterized gingival phenotype. We used immunomorphological, biochemical, and siRNA approaches to analyze gingival tissues and primary cultures of gingival fibroblasts of two unrelated, previously reported RNS patients. We showed that fibrosis, pathological gingival calcifications and increased expression of various profibrotic and pro-osteogenic proteins such as POSTN, SPARC and VIM were common findings. Proteomic analysis of differentially expressed proteins demonstrated that proteins involved in extracellular matrix (ECM) regulation and related to the TGFβ/SMAD signaling pathway were increased. Functional analyses confirmed the upregulation of TGFβ/SMAD signaling and subsequently uncovered the involvement of two closely related transcription cofactors important in fibrogenesis, Yes-associated protein (YAP) and transcriptional coactivator with PDZ-binding motif (TAZ). Knocking down of FAM20C confirmed the TGFβ-YAP/TAZ interplay indicating that a profibrotic loop enabled gingival fibrosis in RNS patients. In summary, our in vivo and in vitro data provide a detailed description of the RNS gingival phenotype. They show that gingival fibrosis and calcifications are associated with, and most likely caused by excessed ECM production and disorganization. They furthermore uncover the contribution of increased TGFβ–YAP/TAZ signaling in the pathogenesis of the gingival fibrosis.
Published: 2024
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3. BacA: a possible regulator that contributes to the biofilm formation of Pseudomonas aeruginosa

Author: Lisa Wallart, Mohamed Amine Ben Mlouka, Brahim Saffiedine, Laurent Coquet, Hung Le, Julie Hardouin, Thierry Jouenne, Gilles Phan, Marie-Christine Kiefer-Meyer, Eric Girard, Isabelle Broutin, and Pascal Cosette
Subjects: Pseudomonas aeruginosa, biofilm, rhamnolipids, proteome, crystallography, Psp system, Microbiology, QR1-502
Abstract: Previously, we pointed out in P. aeruginosa PAO1 biofilm cells the accumulation of a hypothetical protein named PA3731 and showed that the deletion of the corresponding gene impacted its biofilm formation capacity. PA3731 belongs to a cluster of 4 genes (pa3732 to pa3729) that we named bac for “Biofilm Associated Cluster.” The present study focuses on the PA14_16140 protein, i.e., the PA3732 (BacA) homolog in the PA14 strain. The role of BacA in rhamnolipid secretion, biofilm formation and virulence, was confirmed by phenotypic experiments with a bacA mutant. Additional investigations allow to advance that the bac system involves in fact 6 genes organized in operon, i.e., bacA to bacF. At a molecular level, quantitative proteomic studies revealed an accumulation of the BAC cognate partners by the bacA sessile mutant, suggesting a negative control of BacA toward the bac operon. Finally, a first crystallographic structure of BacA was obtained revealing a structure homologous to chaperones or/and regulatory proteins.
Published: 2024
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4. Validation in the ESPOIR cohort of vitamin K-dependent protein S (PROS) as a potential biomarker capable of predicting response to the methotrexate/etanercept combination

Author: Olivier Vittecoq, Clément Guillou, Julie Hardouin, Baptiste Gerard, Francis Berenbaum, Arnaud Constantin, Nathalie Rincheval, Bernard Combe, Thierry Lequerre, and Pascal Cosette
Subjects: PROS, CO7, Prediction, Rheumatoid arthritis, Etanercept, Adalimumab, Diseases of the musculoskeletal system, RC925-935
Abstract: Abstract Background To validate the ability of PROS (vitamin K-dependent protein S) and CO7 (complement component C7) to predict response to the methotrexate (MTX)/etanercept (ETA) combination in rheumatoid arthritis (RA) patients who received this therapeutic combination in a well-documented cohort. Method From the ESPOIR cohort, RA patients having received the MTX/ETA or MTX/adalimumab (ADA) combination as a first-line biologic treatment were included. Serum concentrations of PROS and CO7 were measured by ELISA prior to the initiation of ETA or ADA, at a time where the disease was active (DAS28 ESR > 3.2). The clinical efficacy (response/non-response) of both combinations has been evaluated after at least 6 months of treatment, according to the EULAR response criteria with some modifications. Results Thirty-two were treated by MTX/ETA; the numbers of responders and non-responders were 24 and 8, respectively. Thirty-three patients received the MTX/ADA combination; 27 and 5 patients were respectively responders and non-responders. While there were no differences for demographic, clinical, biological, and X-rays data, as well as for CO7, serum levels of PROS tended to be significantly higher in responders to the MTX/ETA combination (p = 0.08) while no difference was observed in the group receiving MTX/ADA. For PROS, the best concentration threshold to differentiate both groups was calculated at 40 μg/ml using ROC curve. The theranostic performances of PROS appeared better for the ETA/MTX combination. When considering the response to this combination, analysis of pooled data from ESPOIR and SATRAPE (initially used to validate PROS and CO7 as potential theranostic biomarkers) cohorts led to a higher theranostic value of PROS that became significant (p = 0.009). Conclusion PROS might be one candidate of a combination of biomarkers capable of predicting the response to MTX/ETA combination in RA patients refractory to MTX. Trial registration ClinicalTrials.gov identifiers: NCT03666091 and NCT00234234 .
Published: 2022
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5. Hepatoprotective Effect of Grape Seed and Skin Extract Against Lithium Exposure Examined by the Window of Proteomics

Author: Ali Mezni, Olfa Khazri, Frédérique Jarnier, Julie Hardouin, Ferid Limam, Thierry Jouenne, Ezzeddine Aouani, and Pascal Cosette
Subjects: Therapeutics. Pharmacology, RM1-950
Abstract: Context The liver is the organ by which the majority of substances are metabolized, including psychotropic drugs. Lithium (Li) used as drug for many neurological disorders such as bipolar disorders. Objective This study aims to assess lithium toxicity and to evaluate the hepatic-protective properties of a grape skin seed and extract (GSSE). Materials and methods Twenty-four male Wistar rats were exposed for 30 days to either various lithium concentrations, GSSE alone, or lithium supplemented with GSSE. The proteomic analysis revealed alterations of liver protein profiles after lithium treatments that were successfully identified by mass spectrometry. Results Lithium treatment induced an oxidative damage by the alteration of antioxidant enzymes activities such as superoxide dismutase, CAT, and Gpx. The regulated proteins are mainly involved in the respiratory electron transport chain, detoxification processes, ribosomal stress pathway, glycolysis, and cytoskeleton. Proteins were differentially expressed in a dose-dependent manner. Interestingly, GSSE reversed the situation and restored the level of liver proteins whose abundance was modified after lithium treatment, arguing for its protective activity. Conclusion Our data demonstrated the ability of proteomic analysis to underline the toxicity mechanisms of lithium in animal models. Based on these results, GSSE may be envisaged as a nutritional supplement to weaken the liver toxicity of lithium.
Published: 2022
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6. Variability of the response of human vaginal Lactobacillus crispatus to 17β-estradiol

Author: Maximilien Clabaut, Amine M. Boukerb, Amine Ben Mlouka, Amandine Suet, Ali Tahrioui, Julien Verdon, Magalie Barreau, Olivier Maillot, Agathe Le Tirant, Madina Karsybayeva, Coralie Kremser, Gérard Redziniak, Cécile Duclairoir-Poc, Chantal Pichon, Julie Hardouin, Pascal Cosette, Sylvie Chevalier, and Marc G. J. Feuilloley
Subjects: Medicine, Science
Abstract: Abstract We previously showed that the physiological concentration of 17β-estradiol in the vaginal environment is sufficient to affect the membrane dynamics and adhesion phenotype of the Lactobacillus crispatus strain CIP104459. However, L. crispatus is a heterogeneous species. Here, we investigated the effect of 17β-estradiol on the recently isolated L. crispatus vaginal strain V4, related to a cluster distant from CIP104459 and at the limit of being a different subspecies. Grown in the same medium, the two strains expressed a highly similar pool of proteins. However, in contrast to CIP104459, L. crispatus V4 showed high aggregation potential and 17β-estradiol promoted this phenotype. This effect was associated with large changes in cell-surface polarity and Lewis acid/base properties. In addition, we observed no effect on the membrane dynamics, contrary to CIP104459. These results can be explained by differences in the properties and organization of the S layer between the two strains. However, as for CIP104459, 17β-estradiol increased biosurfactant production of L. crispatus V4 and their adhesion to vaginal cells. This suggests that 17β-estradiol agonists would be valuable tools to favor a stable re-implantation of L. crispatus in the vaginal mucosa.
Published: 2021
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7. Phosphorylation of Extracellular Proteins in Acinetobacter baumannii in Sessile Mode of Growth

Author: Sébastien Massier, Brandon Robin, Marianne Mégroz, Amy Wright, Marina Harper, Brooke Hayes, Pascal Cosette, Isabelle Broutin, John D. Boyce, Emmanuelle Dé, and Julie Hardouin
Subjects: phosphorylation, Acinetobacter baumannii, biofilm, extracellular proteins, proteomics, Hcp, Microbiology, QR1-502
Abstract: Acinetobacter baumannii is a problematic nosocomial pathogen owing to its increasing resistance to antibiotics and its great ability to survive in the hospital environment, which is linked to its capacity to form biofilms. Structural and functional investigations of post-translational modifications, such as phosphorylations, may lead to identification of candidates for therapeutic targets against this pathogen. Here, we present the first S/T/Y phosphosecretome of two A. baumannii strains, the reference strain ATCC 17978 and the virulent multi-drug resistant strain AB0057, cultured in two modes of growth (planktonic and biofilm) using TiO2 chromatography followed by high resolution mass spectrometry. In ATCC 17978, we detected a total of 137 (97 phosphoproteins) and 52 (33 phosphoproteins) phosphosites in biofilm and planktonic modes of growth, respectively. Similarly, in AB0057, 155 (119 phosphoproteins) and 102 (74 phosphoproteins) phosphosites in biofilm and planktonic modes of growth were identified, respectively. Both strains in the biofilm mode of growth showed a higher number of phosphosites and phosphoproteins compared to planktonic growth. Several phosphorylated sites are localized in key regions of proteins involved in either drug resistance (β-lactamases), adhesion to host tissues (pilins), or protein secretion (Hcp). Site-directed mutagenesis of the Hcp protein, essential for type VI secretion system-mediated interbacterial competition, showed that four of the modified residues are essential for type VI secretion system activity.
Published: 2021
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8. Anti-Carbamylated Fibrinogen Antibodies Might Be Associated With a Specific Rheumatoid Phenotype and Include a Subset Recognizing In Vivo Epitopes of Its γ Chain One of Which Is Not Cross Reactive With Anti-Citrullinated Protein Antibodies

Author: Pauline Brevet, Claire Lattard, Clément Guillou, Pascal Rottenberg, Patrice Fardellone, Xavier Le-Loët, Thierry Lequerré, Pascal Cosette, Olivier Boyer, Manuel Fréret, and Olivier Vittecoq
Subjects: very early rheumatoid arthritis, anti-carbamylated protein antibodies (anti-CarP), fibrinogen, ACPA, prognosis, Immunologic diseases. Allergy, RC581-607
Abstract: To identify the targets recognized by anti-carbamylated protein antibodies (anti-CarP) in patients with early Rheumatoid Arthritis (RA), to study the cross-reactivity between anti-CarP and anti-citrullinated protein antibodies (ACPA) and to evaluate their prognostic value. 331 patients (184 RA and 147 other rheumatisms) from the Very Early Arthritis (VErA) French cohort were analyzed. We performed mass spectrometry analysis of RA sera displaying anti-CarP activity and epitope mapping of the carbamylated fibrinogen γ chain to identify immunodominant peptides. The specificity of these targets was studied using competition assays with the major antigens recognized by ACPA. The prognostic value of anti-carbamylated fibrinogen IgG antibodies (ACa-Fib IgG) was compared to that of anti-cyclic citrullinated peptide antibodies (anti-CCP) and anti-CarP using an in-house ELISA. Besides the α chain, the γ chain of fibrinogen, particularly one immunodominant epitope that has a specific reactivity, was identified as a circulating carbamylated target in sera. The prevalence of ACa-Fib was 37% at baseline and 10.9% for anti-CCP-negative RA. In anti-CCP-negative patients, ACa-Fib positivity was associated with a more inflammatory and erosive disease at baseline but not with rapid radiological progression, which remains strongly related to anti-CCP antibodies. Fibrinogen seems to be one of the antigens recognized in vivo by the anti-CarP response, particularly 2 epitopes of the γ chain, one of which is not cross reactive with ACPA. This specificity might be associated with a distinct clinical phenotype since ACa-Fib IgG were shown to be linked to systemic inflammation in very early RA but not to rapid radiological progression.
Published: 2021
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9. Pathogenesis of Enamel-Renal Syndrome Associated Gingival Fibromatosis: A Proteomic Approach

Author: Victor Simancas Escorcia, Clément Guillou, Lilia Abbad, Louise Derrien, Claudio Rodrigues Rezende Costa, Vidjea Cannaya, Mourad Benassarou, Christos Chatziantoniou, Ariane Berdal, Ana Carolina Acevedo, Olivier Cases, Pascal Cosette, and Renata Kozyraki
Subjects: FAM20A, FAM20C, secretome analysis, enamel renal syndrome, gingival fibroblast, gingival fibromatosis, Diseases of the endocrine glands. Clinical endocrinology, RC648-665
Abstract: The enamel renal syndrome (ERS) is a rare disorder featured by amelogenesis imperfecta, gingival fibromatosis and nephrocalcinosis. ERS is caused by bi-allelic mutations in the secretory pathway pseudokinase FAM20A. How mutations in FAM20A may modify the gingival connective tissue homeostasis and cause fibromatosis is currently unknown. We here analyzed conditioned media of gingival fibroblasts (GFs) obtained from four unrelated ERS patients carrying distinct mutations and control subjects. Secretomic analysis identified 109 dysregulated proteins whose abundance had increased (69 proteins) or decreased (40 proteins) at least 1.5-fold compared to control GFs. Proteins over-represented were mainly involved in extracellular matrix organization, collagen fibril assembly, and biomineralization whereas those under-represented were extracellular matrix-associated proteins. More specifically, transforming growth factor-beta 2, a member of the TGFβ family involved in both mineralization and fibrosis was strongly increased in samples from GFs of ERS patients and so were various known targets of the TGFβ signaling pathway including Collagens, Matrix metallopeptidase 2 and Fibronectin. For the over-expressed proteins quantitative RT-PCR analysis showed increased transcript levels, suggesting increased synthesis and this was further confirmed at the tissue level. Additional immunohistochemical and western blot analyses showed activation and nuclear localization of the classical TGFβ effector phospho-Smad3 in both ERS gingival tissue and ERS GFs. Exposure of the mutant cells to TGFB1 further upregulated the expression of TGFβ targets suggesting that this pathway could be a central player in the pathogenesis of the ERS gingival fibromatosis.In conclusion our data strongly suggest that TGFβ -induced modifications of the extracellular matrix contribute to the pathogenesis of ERS. To our knowledge this is the first proteomic-based analysis of FAM20A-associated modifications.
Published: 2021
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10. Elicitation of Roots and AC-DC with PEP-13 Peptide Shows Differential Defense Responses in Multi-Omics

Author: Marie Chambard, Mohamed Amine Ben Mlouka, Lun Jing, Carole Plasson, Pascal Cosette, Jérôme Leprince, Marie-Laure Follet-Gueye, Azeddine Driouich, Eric Nguema-Ona, and Isabelle Boulogne
Subjects: root-associated cap-derived cells (root AC-DC), omics, PEP-13 elicitor, Glycine max, Cytology, QH573-671
Abstract: The root extracellular trap (RET) has emerged as a specialized compartment consisting of root AC-DC and mucilage. However, the RET’s contribution to plant defense is still poorly understood. While the roles of polysaccharides and glycoproteins secreted by root AC-DC have started to be elucidated, how the low-molecular-weight exudates of the RET contribute to root defense is poorly known. In order to better understand the RET and its defense response, the transcriptomes, proteomes and metabolomes of roots, root AC-DC and mucilage of soybean (Glycine max (L.) Merr, var. Castetis) upon elicitation with the peptide PEP-13 were investigated. This peptide is derived from the pathogenic oomycete Phytophthora sojae. In this study, the root and the RET responses to elicitation were dissected and sequenced using transcriptional, proteomic and metabolomic approaches. The major finding is increased synthesis and secretion of specialized metabolites upon induced defense activation following PEP-13 peptide elicitation. This study provides novel findings related to the pivotal role of the root extracellular trap in root defense.
Published: 2022
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11. Proteomic and transcriptomic study of brain microvessels in neonatal and adult mice.

Author: Baptiste Porte, Clémence Chatelain, Julie Hardouin, Céline Derambure, Yasmine Zerdoumi, Michèle Hauchecorne, Nicolas Dupré, Soumeya Bekri, Bruno Gonzalez, Stéphane Marret, Pascal Cosette, and Philippe Leroux
Subjects: Medicine, Science
Abstract: Infants born before 29 weeks gestation incur a major risk of preterm encephalopathy and subependymal/intracerebral/intraventricular haemorrhage. In mice, an ontogenic window of haemorrhage risk was recorded up to 5 days after birth in serpine1 knock-out animals. Using proteome and transcriptome approaches in mouse forebrain microvessels, we previously described the remodelling of extracellular matrix and integrins likely strengthening the vascular wall between postnatal day 5 (P5) and P10. Haemorrhage is the ultimate outcome of vessel damage (i.e., during ischaemia), although discreet vessel insults may be involved in the aetiology of preterm encephalopathy. In this study, we examined proteins identified by mass spectrometry and segregating in gene ontology pathways in forebrain microvessels in P5, P10, and adult wild type mice. In parallel, comparative transcript levels were obtained using RNA hybridization microarrays and enriched biological pathways were extracted from genes exhibiting at least a two-fold change in expression. Five major biological functions were observed in those genes detected both as proteins and mRNA expression undergoing at least a two-fold change in expression in one or more age comparisons: energy metabolism, protein metabolism, antioxidant function, ion exchanges, and transport. Adult microvessels exhibited the highest protein and mRNA expression levels for a majority of genes. Energy metabolism-enriched gene ontology pathways pointed to the preferential occurrence of glycolysis in P5 microvessels cells versus P10 and adult preparations enriched in aerobic oxidative enzymes. Age-dependent levels of RNA coding transport proteins at the plasma membrane and mitochondria strengthened our findings based on protein data. The data suggest that immature microvessels have fewer energy supply alternatives to glycolysis than mature structures. In the context of high energy demand, this constraint might account for vascular damage and maintenance of the high bleeding occurrence in specific areas in immature brain.
Published: 2017
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12. Foxg1-Cre Mediated Lrp2 Inactivation in the Developing Mouse Neural Retina, Ciliary and Retinal Pigment Epithelia Models Congenital High Myopia.

Author: Olivier Cases, Antoine Joseph, Antoine Obry, Mathieu D Santin, Sirine Ben-Yacoub, Michel Pâques, Sabine Amsellem-Levera, Ana Bribian, Manuel Simonutti, Sébastien Augustin, Thomas Debeir, José Alain Sahel, Annabel Christ, Fernando de Castro, Stéphane Lehéricy, Pascal Cosette, and Renata Kozyraki
Subjects: Medicine, Science
Abstract: Myopia is a common ocular disorder generally due to increased axial length of the eye-globe. Its extreme form high myopia (HM) is a multifactorial disease leading to retinal and scleral damage, visual impairment or loss and is an important health issue. Mutations in the endocytic receptor LRP2 gene result in Donnai-Barrow (DBS) and Stickler syndromes, both characterized by HM. To clearly establish the link between Lrp2 and congenital HM we inactivated Lrp2 in the mouse forebrain including the neural retina and the retinal and ciliary pigment epithelia. High resolution in vivo MRI imaging and ophthalmological analyses showed that the adult Lrp2-deficient eyes were 40% longer than the control ones mainly due to an excessive elongation of the vitreal chamber. They had an apparently normal intraocular pressure and developed chorioretinal atrophy and posterior scleral staphyloma features reminiscent of human myopic retinopathy. Immunomorphological and ultrastructural analyses showed that increased eye lengthening was first observed by post-natal day 5 (P5) and that it was accompanied by a rapid decrease of the bipolar, photoreceptor and retinal ganglion cells, and eventually the optic nerve axons. It was followed by scleral thinning and collagen fiber disorganization, essentially in the posterior pole. We conclude that the function of LRP2 in the ocular tissues is necessary for normal eye growth and that the Lrp2-deficient eyes provide a unique tool to further study human HM.
Published: 2015
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13. Escherichia coli response to uranyl exposure at low pH and associated protein regulations.

Author: Arbia Khemiri, Marie Carrière, Nicolas Bremond, Mohamed Amine Ben Mlouka, Laurent Coquet, Isabelle Llorens, Virginie Chapon, Thierry Jouenne, Pascal Cosette, and Catherine Berthomieu
Subjects: Medicine, Science
Abstract: Better understanding of uranyl toxicity in bacteria is necessary to optimize strains for bioremediation purposes or for using bacteria as biodetectors for bioavailable uranyl. In this study, after different steps of optimization, Escherichia coli cells were exposed to uranyl at low pH to minimize uranyl precipitation and to increase its bioavailability. Bacteria were adapted to mid acidic pH before exposure to 50 or 80 µM uranyl acetate for two hours at pH≈3. To evaluate the impact of uranium, growth in these conditions were compared and the same rates of cells survival were observed in control and uranyl exposed cultures. Additionally, this impact was analyzed by two-dimensional differential gel electrophoresis proteomics to discover protein actors specifically present or accumulated in contact with uranium.Exposure to uranium resulted in differential accumulation of proteins associated with oxidative stress and in the accumulation of the NADH/quinone oxidoreductase WrbA. This FMN dependent protein performs obligate two-electron reduction of quinones, and may be involved in cells response to oxidative stress. Interestingly, this WrbA protein presents similarities with the chromate reductase from E. coli, which was shown to reduce uranyl in vitro.
Published: 2014
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14. Identification of S100A9 as biomarker of responsiveness to the methotrexate/etanercept combination in rheumatoid arthritis using a proteomic approach.

Author: Antoine Obry, Thierry Lequerré, Julie Hardouin, Olivier Boyer, Patrice Fardellone, Peggy Philippe, Xavier Le Loët, Pascal Cosette, and Olivier Vittecoq
Subjects: Medicine, Science
Abstract: One way to optimize the drug prescription in rheumatoid arthritis (RA) is to identify predictive biomarkers of drug responsiveness. Here, we investigated the potential "theranostic" value of proteins of the S100 family by monitoring levels of both S100A8 and S100A9 in blood samples from RA patients.For proteomic analysis, peripheral blood mononuclear cells (PBMC) and serum samples were collected in patients prior to initiation of the methotrexate/etanercept (MTX/ETA) combination. Firstly, relative mass spectrometry (MS) quantification focusing on S100A8 and S100A9 proteins was carried out from PBMCs samples to identify potential biomarkers. The same approach was also performed from serum samples from responder (R) and non responder (NR) patients. Finally, to confirm these results, an absolute quantification of S100A8, S100A9 proteins and calprotectin (heterodimer of S100A8/S100A9) was carried out on the serum samples using ELISA.MS analyses revealed that both S100A8 and S100A9 proteins were significantly accumulated in PBMC from responders. In contrast to PBMC, only the S100A9 protein was significantly overexpressed in the serum of R patients. Absolute quantification by ELISA confirmed this result and pointed out a similar expression level of S100A8 protein and calprotectin in sera from both R and NR groups. Thus, the S100A9 protein revealed to be predictive of MTX/ETA responsiveness, contrarily to parameters of inflammation and auto-antibodies which did not allow significant discrimination.This is the first report of an overexpression of S100A9 protein in both PBMCs and serum of patients with subsequent response to the MTX/ETA combination. This protein thus represents an interesting biomarker candidate of therapeutic response in RA.
Published: 2014
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15. Identification of biofilm-associated cluster (bac) in Pseudomonas aeruginosa involved in biofilm formation and virulence.

Author: Camille Macé, Damien Seyer, Chanez Chemani, Pascal Cosette, Patrick Di-Martino, Benoit Guery, Alain Filloux, Marc Fontaine, Virginie Molle, Guy-Alain Junter, and Thierry Jouenne
Subjects: Medicine, Science
Abstract: Biofilms are prevalent in diseases caused by Pseudomonas aeruginosa, an opportunistic and nosocomial pathogen. By a proteomic approach, we previously identified a hypothetical protein of P. aeruginosa (coded by the gene pA3731) that was accumulated by biofilm cells. We report here that a Delta pA3731 mutant is highly biofilm-defective as compared with the wild-type strain. Using a mouse model of lung infection, we show that the mutation also induces a defect in bacterial growth during the acute phase of infection and an attenuation of the virulence. The pA3731 gene is found to control positively the ability to swarm and to produce extracellular rhamnolipids, and belongs to a cluster of 4 genes (pA3729-pA3732) not previously described in P. aeruginosa. Though the protein PA3731 has a predicted secondary structure similar to that of the Phage Shock Protein, some obvious differences are observed compared to already described psp systems, e.g., this unknown cluster is monocistronic and no homology is found between the other proteins constituting this locus and psp proteins. As E. coli PspA, the amount of the protein PA3731 is enlarged by an osmotic shock, however, not affected by a heat shock. We consequently named this locus bac for biofilm-associated cluster.
Published: 2008
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16. Purification and characterization of a novel high molecular weight alkaline protease produced by an endophytic Bacillus halotolerans strain CT2

Author: Dorra, Gharbi, Ines, Karkouch, Imen, Ben Slimene, Laurent, Coquet, Sana, Azaiez, Olfa, Tabbene, Pascal, Cosette, Thierry, Jouenne, and Ferid, Limam
Published: 2018
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17. Physiological and proteomic analyses of Tunisian local grapevine (

Author: Rahma Jardak, Jawaher Riahi, Clément Guillou, Pascal Cosette, Wassim Azri, and Ahmed Mliki
Subjects: fungi, Drought tolerance, food and beverages, Plant Science, Oxidative phosphorylation, Carbohydrate metabolism, Biology, Photosynthesis, Acclimatization, Botany, Protein biosynthesis, Photorespiration, Osmoprotectant, Agronomy and Crop Science
Abstract: Drought is one of the major environmental constraints threatening viticulture worldwide. Therefore, it is critical to reveal the molecular mechanisms underlying grapevine (Vitis vinifera L.) drought stress tolerance useful to select new species with higher tolerance/resilience potentials. Drought-tolerant Tunisian local grapevine cultivar Razegui was exposed to water deficit for 16 days. Subsequent proteomic analysis revealed 49 differentially accumulated proteins in leaves harvested on the drought-stressed vines. These proteins were mainly involved in photosynthesis, stress defence, energy and carbohydrate metabolism, protein synthesis/turnover and amino acid metabolism. Physiological analysis revealed that reduction of photosynthesis under drought stress was attributed to the downregulation of the light-dependent reactions, Calvin cycle and key enzymes of the photorespiration pathway. The accumulation of proteins involved in energy and carbohydrate metabolism indicate enhanced need of energy during active stress acclimation. Accumulation of protein amino acids seems to play a protective role under drought stress due to their osmoprotectant and ROS scavenging potential. Reduced protein synthesis and turnover help plants preserving energy to fight drought stress. Proteins related to stress defence might scavenge ROS and transmit the ROS signal as an oxidative signal transducer in drought-stress signalling. All of these original results represent valuable information towards improving drought tolerance of grapevine and promoting sustainable viticulture under climate change conditions.
Published: 2021
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18. Physiological and proteomic responses to drought stress in leaves of two wild grapevines (Vitis sylvestris): a comparative study

Author: Ahmed Mliki, Pascal Cosette, Wassim Azri, Zouheir Nasr, Mokded Rabhi, and Clément Guillou
Subjects: 0106 biological sciences, 0301 basic medicine, Drought stress, biology, Physiology, fungi, RuBisCO, Drought tolerance, food and beverages, Plant physiology, Plant Science, APX, Photosynthesis, 01 natural sciences, 03 medical and health sciences, 030104 developmental biology, Botany, biology.protein, Cultivar, Agronomy and Crop Science, Gene, 010606 plant biology & botany
Abstract: Grapevine is one of the most important fruit crops in the world, which is severely threatened by drought. Therefore, understanding grapevine drought response mechanisms is needed to develop grapevine cultivars that can tolerate this stress. In the present report, a comparative proteomic study using 2D-PAGE was performed on two wild grapevine accessions, Tebaba (salt tolerant) and Houamdia (salt sensitive), to identify proteins that play key roles in drought responsive mechanisms. Plants were exposed to water deficit stress for 16 days. Physiological observations did not indicate any difference in drought tolerance between the two accessions. However, the comparative proteomic study showed that 18 drought-responsive proteins changed in both accessions under drought stress and 48 (29 in Houamdia and 19 in Tebaba) were variety specific. Based on changes in protein abundance induced by drought stress, carbohydrate and energy metabolism were similarly up-regulated in both accessions. Amino acid metabolism was more negatively affected by the stress in Houamdia accession. Interestingly, the three ROS scavenging proteins APX, ASR2 and GRXS17 were up-regulated only in Tebaba. Some drought-responsive proteins, such as RBP, RuBisCO, RCA, 26S protease, CLpA and 14–3-3-like protein were up-regulated by the stress in Tebaba, whereas they were down-regulated in Houamdia. Taken together, these results suggest that Tebaba may alleviate drought stress through an activation of photosynthesis and redox reactions, and a degradation of misfolded/damaged proteins. Information given in this report could be helpful for selecting candidate proteins/genes as markers in improving drought tolerance in grapevine cultivars.
Published: 2020
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19. Rapid evolution of pollen and pistil traits as a response to sexual selection in the post-pollination phase of mating

Author: Jeanne Tonnabel, Pascal Cosette, Arnaud Lehner, Jean-Claude Mollet, Mohamed Amine Ben Mlouka, Lucija Grladinovic, Patrice David, and John R. Pannell
Subjects: Male, Sexual Selection, Reproduction, Seeds, Animals, Pollen, Female, Flowers, Plants, General Agricultural and Biological Sciences, Pollination, General Biochemistry, Genetics and Molecular Biology
Abstract: Sexual selection is the basis of some of the most striking phenotypic variation in nature.
Published: 2022

20. Variability of the response of human vaginal Lactobacillus crispatus to 17β-estradiol

Author: Sylvie Chevalier, Maximilien Clabaut, Magalie Barreau, Gérard Redziniak, Madina Karsybayeva, Marc G. J. Feuilloley, Julie Hardouin, Agathe Le Tirant, Amine M. Boukerb, Cécile Duclairoir-Poc, Olivier Maillot, Amandine Suet, Amine Ben Mlouka, Julien Verdon, Pascal Cosette, Chantal Pichon, Coralie Kremser, Ali Tahrioui, Ecologie et biologie des interactions (EBI), Université de Poitiers-Centre National de la Recherche Scientifique (CNRS), Microbiologie de l'Eau (MDE), and Université de Poitiers-Centre National de la Recherche Scientifique (CNRS)-Université de Poitiers-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Physiology, Science, [SDV]Life Sciences [q-bio], 030106 microbiology, Microbiology, Article, 03 medical and health sciences, Membrane dynamics, Humans, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Lactobacillus crispatus, Multidisciplinary, Strain (chemistry), biology, Estradiol, Chemistry, Vaginal mucosa, Adhesion, biology.organism_classification, Phenotype, 030104 developmental biology, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Vagina, Medicine, Female, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, S-layer
Abstract: We previously showed that the physiological concentration of 17β-estradiol in the vaginal environment is sufficient to affect the membrane dynamics and adhesion phenotype of the Lactobacillus crispatus strain CIP104459. However, L. crispatus is a heterogeneous species. Here, we investigated the effect of 17β-estradiol on the recently isolated L. crispatus vaginal strain V4, related to a cluster distant from CIP104459 and at the limit of being a different subspecies. Grown in the same medium, the two strains expressed a highly similar pool of proteins. However, in contrast to CIP104459, L. crispatus V4 showed high aggregation potential and 17β-estradiol promoted this phenotype. This effect was associated with large changes in cell-surface polarity and Lewis acid/base properties. In addition, we observed no effect on the membrane dynamics, contrary to CIP104459. These results can be explained by differences in the properties and organization of the S layer between the two strains. However, as for CIP104459, 17β-estradiol increased biosurfactant production of L. crispatus V4 and their adhesion to vaginal cells. This suggests that 17β-estradiol agonists would be valuable tools to favor a stable re-implantation of L. crispatus in the vaginal mucosa.
Published: 2021
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21. LasB and CbpD Virulence Factors of Pseudomonas aeruginosa Carry Multiple Post-Translational Modifications on Their Lysine Residues

Author: Pascal Cosette, Charlotte Gaviard, Julie Hardouin, Thierry Jouenne, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)
Subjects: Virulence Factors, Lysine, Virulence, Human pathogen, Biology, medicine.disease_cause, Biochemistry, Microbiology, 03 medical and health sciences, Succinylation, Bacterial Proteins, medicine, [CHIM]Chemical Sciences, Humans, Electrophoresis, Gel, Two-Dimensional, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Pseudomonas aeruginosa, 030302 biochemistry & molecular biology, Metalloendopeptidases, General Chemistry, Lysine residue, 3. Good health, Acetylation, Posttranslational modification, [CHIM.OTHE]Chemical Sciences/Other, Carrier Proteins, Protein Processing, Post-Translational
Abstract: Pseudomonas aeruginosa is a multi-drug resistant human pathogen largely involved in nosocomial infections. Today, effective antibacterial agents are lacking. Exploring the bacterial physiology at the post-translational modifications (PTM) level may contribute to the renewal of fighting strategies. Indeed, some correlations between PTMs and the bacterial virulence, adaptation, and resistance have been shown. In a previous study performed in P. aeruginosa, we reported that many virulence factors like chitin-binding protein CbpD and elastase LasB were multiphosphorylated. Besides phosphorylation, other PTMs, like those occurring on lysine, seem to play key roles in bacteria. In the present study, we investigated for the first time the lysine succinylome and acetylome of the extracellular compartment of P. aeruginosa by using a two-dimensional immunoaffinity approach. Some virulence factors were identified as multimodified on lysine residues, among them, LasB and CbpD. Lysine can be modified by a wide range of chemical groups. In order to check the presence of other chemical groups on modified lysines identified on LasB and CbpD, we used 1- and 2- dimensional gel electrophoresis approaches to target lysine modified by 7 other modifications: butyrylation, crotonylation, dimethylation, malonylation, methylation, propionylation, and trimethylation. We showed that some lysines of these two virulence factors were modified by these 9 different PTMs. Interestingly, we found that the PTMs recovered on these two virulence factors were different than those previously reported in the intracellular compartment.
Published: 2019
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22. Facteurs prédictifs de réponses dans la polyarthrite rhumatoïde

Author: Pascal Rottenberg, Céline Derambure, Thierry Lequerré, Pascal Cosette, Olivier Vittecoq, Physiopathologie, Autoimmunité, maladies Neuromusculaires et THErapies Régénératrices (PANTHER), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Génomique et Médecine Personnalisée du Cancer et des Maladies Neuropsychiatriques (GPMCND), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 030203 arthritis & rheumatology, 0303 health sciences, 03 medical and health sciences, 0302 clinical medicine, Rheumatology, [SDV]Life Sciences [q-bio], 030304 developmental biology, 3. Good health
Abstract: Resume L’accroissement du nombre de molecules disponibles pour le traitement de la polyarthrite rhumatoide incite les rhumatologues a identifier et valider des biomarqueurs de reponse ou biomarqueurs theranostiques, capables de predire la reponse aux traitements, prealablement a toute exposition. Cette demarche s’inscrit dans le contexte de medecine personnalisee afin de traiter efficacement un patient donne et a un instant donne. Les anticorps anti-peptides citrullines, les facteurs rhumatoides et la signature interferon sont les biomarqueurs les plus robustes et valides parmi tous ceux identifies. Les matrices utilisant des parametres cliniques ou biologiques, diagnostiques ou pronostiques, semblent pertinentes pour definir un traitement a l’echelon individuel. Par ailleurs, le developpement des approches a grande echelle sans a priori, comme la genomique fonctionnelle ou la metabolomique, representent une voie de recherche tout a fait prometteuse, bien que la replication des resultats reste difficile. La complexite de la reponse therapeutique chez un meme patient et la variabilite interindividuelle incitent a identifier des combinaisons de biomarqueurs plutot qu’un seul biomarqueur. L’objectif de cette revue est de faire le point sur les differentes approches utilisees pour identifier des biomarqueurs theranostiques et de recenser l’ensemble des biomarqueurs disponibles en discutant de leur performance en pratique clinique. Cependant, le nombre de biomarqueurs actuellement utilisables en pratique quotidienne reste tres limite.
Published: 2019
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23. Protective effect of grape seed and skin extract on cerebral ischemia in rat: implication of transition metals

Author: Safwen, Kadri, Selima, Smine, Mohamed, Elayed, Ferid, Limam, Pascal, Cosette, Mohamed, Amri, Ezzedine, Aouani, and Meherzia, Mokni
Published: 2015
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24. 3-Benzoylquinoxalinone as a photoaffinity labelling derivative with fluorogenic properties allowing reaction monitoring under 'no-wash' conditions

Author: Clément Guillou, Pascal Cosette, Magalie Bénard, Pierre-Yves Renard, Madeleine Cauwel, Damien Schapman, Kévin Renault, Ludovic Galas, Cyrille Sabot, Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Université de Rouen Normandie (UNIROUEN), and Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Metals and Alloys, General Chemistry, 010402 general chemistry, 01 natural sciences, Fluorescence, Combinatorial chemistry, Catalysis, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, chemistry.chemical_compound, chemistry, Covalent bond, Labelling, Materials Chemistry, Ceramics and Composites, Derivative (chemistry)
Abstract: Described herein is a quinoxalinone-based photoaffinity probe with caged fluorescence properties. Upon visible blue LED irradiation (λmax 450 nm), this photo-crosslinker is able to covalently capture proteins with concomitant fluorescence labelling. This process enables monitoring applications under “no wash” conditions.
Published: 2021
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25. Physiological and proteomic analyses of Tunisian local grapevine (Vitis vinifera) cultivar Razegui in response to drought stress

Author: Wassim, Azri, Rahma, Jardak, Pascal, Cosette, Clément, Guillou, Jawaher, Riahi, and Ahmed, Mliki
Subjects: Plant Leaves, Proteomics, Vitis, Photosynthesis, Droughts
Abstract: Drought is one of the major environmental constraints threatening viticulture worldwide. Therefore, it is critical to reveal the molecular mechanisms underlying grapevine (Vitis vinifera L.) drought stress tolerance useful to select new species with higher tolerance/resilience potentials. Drought-tolerant Tunisian local grapevine cultivar Razegui was exposed to water deficit for 16days. Subsequent proteomic analysis revealed 49 differentially accumulated proteins in leaves harvested on the drought-stressed vines. These proteins were mainly involved in photosynthesis, stress defence, energy and carbohydrate metabolism, protein synthesis/turnover and amino acid metabolism. Physiological analysis revealed that reduction of photosynthesis under drought stress was attributed to the downregulation of the light-dependent reactions, Calvin cycle and key enzymes of the photorespiration pathway. The accumulation of proteins involved in energy and carbohydrate metabolism indicate enhanced need of energy during active stress acclimation. Accumulation of protein amino acids seems to play a protective role under drought stress due to their osmoprotectant and ROS scavenging potential. Reduced protein synthesis and turnover help plants preserving energy to fight drought stress. Proteins related to stress defence might scavenge ROS and transmit the ROS signal as an oxidative signal transducer in drought-stress signalling. All of these original results represent valuable information towards improving drought tolerance of grapevine and promoting sustainable viticulture under climate change conditions.
Published: 2021

26. Antioxidant, antityrosinase and antibiofilm activities of synthesized peptides derived from Vicia faba protein hydrolysate: A powerful agents in cosmetic application

Author: Ines Karkouch, Mohamed Amine Ben Mlouka, Pascal Cosette, Ferid Limam, Christophe Rihouey, Salem Elkahoui, Dorra Gharbi, Laurent Coquet, Thierry Jouenne, Olfa Tabbene, Equipe de recherche sur les relations matrice extracellulaire-cellules (ERRMECe), Fédération INSTITUT DES MATÉRIAUX DE CERGY-PONTOISE (I-MAT), Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, 2. Zero hunger, chemistry.chemical_classification, DPPH, [SDV]Life Sciences [q-bio], Tyrosinase, Peptide, 04 agricultural and veterinary sciences, Tandem mass spectrometry, Trypsin, 040401 food science, Hydrolysate, Vicia faba, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, 0404 agricultural biotechnology, chemistry, Biochemistry, Vicilin, medicine, Agronomy and Crop Science, ComputingMilieux_MISCELLANEOUS, medicine.drug
Abstract: The aim of this study was to identify peptides with antioxidant, antityrosinase and antibiofilm activities released from Vicia faba seed proteins hydrolysate. The hydrolysis pattern was performed with trypsin. Firstly, the obtained hydrolysate was fractionated by cation exchange chromatography and the fraction exhibiting the highest biological activity was then analyzed by reverse phase HPLC tandem mass spectrometry. After annotation by Peaks software (BSI, Canada) for de novo peptide sequencing, seven peptides were identified, mainly derived from storage proteins: legumin and vicilin. These peptides were further chemically synthesized to assess their antioxidant capacity, antityrosinase activity and antibiofilm ability against Pseudomonas aeruginosa PA14. Results showed that peptides P5, P6 and P7 identified as LSPGDVLVIPAGYPVAIK, VESEAGLTETWNPNHPELR and EEYDEEKEQGEEEIR respectively, displayed the highest DPPH radical scavenging activity (IC 50 = 0.25–1.9 mM). P5 was the only peptide able to chelate iron and reduce Fe 3+ to Fe 2+ . Furthermore, peptides P4 (GPLVHPQSQSQSN) and P6 were observed as potent tyrosinase inhibitors with IC 50 values of 1 and 0.14 mM respectively. P1, P5, P6 and P7 also showed interesting antibiofilm activity against Pseudomonas aeruginosa PA14 with MBIC 50 value ranged from 12 to 35 μM. Our data suggest that V. faba seed proteins hydrolysate could be potentially used as a source of natural bioactive peptides for cosmetic and pharmaceutical applications.
Published: 2017
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27. Phospho-secretome characterization of Acinetobacter baumannii in biofilm

Author: Sébastien Massier, Brandon ROBIN, Pascal Cosette, Jouenne, T., Emmanuelle Dé, Julie Hardouin, Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-CRLCC Henri Becquerel-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Polymères Biopolymères Surfaces (PBS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Normandie Université (NU), Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de la Recherche Agronomique (INRA), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-CHU Rouen, Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Institut National de la Recherche Agronomique (INRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), and Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Subjects: [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract: International audience
Published: 2019

28. Neuroprotective effect of grape seed extract on brain ischemia: a proteomic approach

Author: Salem Elkhaoui, Sami Zekri, Ferid Limam, Mohamed El Ayed, Meherzia Mokni, Pascal Cosette, Safwen Kadri, Ezzedine Aouani, Thierry Jouenne, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Faculté de Médecine de Tunis, Université de Tunis El Manar (UTM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Faculté des Sciences de Bizerte [Université de Carthage], and Université de Carthage - University of Carthage
Subjects: Male, Proteomics, 0301 basic medicine, food.ingredient, Ischemia, Down-Regulation, Hippocampal formation, Biology, Pharmacology, medicine.disease_cause, Biochemistry, Neuroprotection, Antioxidants, Brain Ischemia, Rats, Sprague-Dawley, Brain ischemia, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, food, medicine, Animals, ComputingMilieux_MISCELLANEOUS, Grape Seed Extract, Dentate gyrus, Brain, medicine.disease, 3. Good health, Oxidative Stress, Neuroprotective Agents, 030104 developmental biology, Reperfusion Injury, Grape seed extract, Proteome, Neurology (clinical), [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress
Abstract: Stroke is one of the leading causes of long-lasting disability in human and oxidative stress an important underlying cause. Molecular insights into pathophysiology of ischemic stroke are still obscure, and the present study investigated the protective effect of high dosage Grape Seed Extract (GSE 2.5 g/kg) on brain ischemia-reperfusion (I/R) injury using a proteomic approach. Ischemia was realized by occlusion of the common carotid arteries for 30 min followed by 1 h reperfusion on control or GSE pre-treated rats, and a label-free quantification followed by mass spectrometry analysis used to evaluate I/R induced alterations in protein abundance and metabolic pathways as well as the protection afforded by GSE. I/R-induced whole brain ionogram dyshomeostasis, ultrastructural alterations, as well as inflammation into hippocampal dentate gyrus area, which were evaluated using ICP-OES, transmission electron microscopy and immuno-histochemistry respectively. I/R altered the whole brain proteome abundance among which 108 proteins were significantly modified (35 up and 73 down-regulated proteins). Eighty-four proteins were protected upon GSE treatment among which 27 were up and 57 down-regulated proteins, suggesting a potent protective effect of GSE close to 78%of the disturbed proteome. Furthermore, GSE efficiently prevented the brain from I/R-induced ion dyshomeostasis, ultrastructural alterations, inflammatory biomarkers as CD56 or CD68 and calcium burst within the hippocampus. To conclude, a potent protective effect of GSE on brain ischemia is evidenced and clinical trials using high dosage GSE should be envisaged on people at high risk for stroke.
Published: 2019
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29. Utilization of Grape Seed Flour for Antimicrobial Lipopeptide Production by Bacillus amyloliquefaciens C5 Strain

Author: Siwar Soussi, Thierry Jouenne, Ferid Limam, Julie Hardouin, Dorra Gharbi, Olfa Tabbene, Pascal Cosette, Rym Essid, Salem Elkahoui, Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0106 biological sciences, Grape seed flour, Bacillus amyloliquefaciens, M9 mineral medium, [SDV]Life Sciences [q-bio], Flour, Bioengineering, Microbial Sensitivity Tests, Antimicrobial activity, 01 natural sciences, Applied Microbiology and Biotechnology, Biochemistry, Lipopeptide, Lipopeptides, Bacillomycin, chemistry.chemical_compound, Anti-Infective Agents, 010608 biotechnology, Vitis, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Food science, Molecular Biology, Strain (chemistry), biology, 010405 organic chemistry, General Medicine, biology.organism_classification, Antimicrobial, Thin-layer chromatography, 0104 chemical sciences, MALDI-TOF/MS, chemistry, Seeds, Antibacterial activity, Surfactin, Biotechnology
Abstract: International audience; An endophytic Bacillus amyloliquefaciens strain called C5, able to produce biosurfactant lipopeptides with a broad antibacterial activity spectrum, has been isolated from the roots of olive tree. Optimization of antibacterial activity was undertaken using grape seed flour (GSF) substrate at 0.02, 0.2, and 2% (w/v) in M9 medium. Strain C5 exhibited optimal growth and antimicrobial activity (MIC value of 60 μg/ml) when incubated in the presence of 0.2% GSF while lipopeptide production culminated at 2% GSF. Thin layer chromatography analysis of lipopeptide extract revealed the presence of at least three active spots at Rf 0.35, 0.59, and 0.72 at 0.2% GSF. Data were similar to those obtained in LB-rich medium. MALDI-TOF/MS analysis of lipopeptide extract obtained from 0.2% GSF substrate revealed the presence of surfactin and bacillomycin D. These results show that GSF could be used as a low-cost culture medium supplement for optimizing the production of biosurfactants by strain C5.
Published: 2019
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30. Predictors of treatment response in rheumatoid arthritis

Author: Pascal Cosette, Céline Derambure, Olivier Vittecoq, Thierry Lequerré, Pascal Rottenberg, CHU Bois-Guillaume, UNIROUEN - UFR Santé (UNIROUEN UFR Santé), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Génomique et Médecine Personnalisée du Cancer et des Maladies Neuropsychiatriques (GPMCND), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de rhumatologie [CHU Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and CCSD, Accord Elsevier
Subjects: Drug, Male, medicine.medical_specialty, Treatment response, [SDV.IMM] Life Sciences [q-bio]/Immunology, Proteome, media_common.quotation_subject, Risk Assessment, Severity of Illness Index, Arthritis, Rheumatoid, 03 medical and health sciences, 0302 clinical medicine, Rheumatology, Predictive Value of Tests, Rheumatoid Factor, Response prediction, medicine, Rheumatoid factor, Humans, 030212 general & internal medicine, Precision Medicine, Rheumatoid arthritis, Intensive care medicine, media_common, 030203 arthritis & rheumatology, [SDV.MHEP.RSOA] Life Sciences [q-bio]/Human health and pathology/Rhumatology and musculoskeletal system, Biological Products, business.industry, medicine.disease, Prognosis, Theranostics, 3. Good health, Review article, Clinical Practice, Treatment Outcome, [SDV.MHEP.RSOA]Life Sciences [q-bio]/Human health and pathology/Rhumatology and musculoskeletal system, Antirheumatic Agents, [SDV.IMM]Life Sciences [q-bio]/Immunology, Identification (biology), Drug Therapy, Combination, Female, Personalized medicine, Patient Safety, business, Transcriptome, Biomarkers
Abstract: International audience; The expanding array of drugs available for treating rheumatoid arthritis is creating challenges in drug selection for the individual patient. The identification of biomarkers that predict the treatment response prior to drug exposure is therefore a current priority. This new approach, known as theranostics, is a component of personalized medicine, which involves selecting the management strategies that are most effective for a given patient at a given point in time. Antibodies to citrullinated peptides, rheumatoid factor, and the interferon signature are the most robust and best validated biomarkers identified to date. Matrices containing clinical or laboratory parameters of diagnostic or prognostic relevance may help to select the best treatment for the individual patient. Furthermore, the development of large-scale approaches requiring no a priori knowledge, such as functional genomics and metabolomics, hold considerable promise, despite persistent difficulties in replicating findings. The complexity of the treatment response in a given patient and substantial variability across patients suggest that biomarkers may be more helpful in combination than singly. The objectives of this review article are to discuss the approaches used to identify theranostic biomarkers and to present an overview of currently available biomarkers and of their performance in everyday clinical practice. However, the range of biomarkers suitable for use in daily practice remains extremely narrow.
Published: 2019
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31. Lysine Succinylation and Acetylation in Pseudomonas aeruginosa

Author: Charlotte Gaviard, Thierry Jouenne, Isabelle Broutin, Julie Hardouin, Emmanuelle Dé, Pascal Cosette, Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Polymères Biopolymères Surfaces (PBS), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), and Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN)
Subjects: 0301 basic medicine, Proteomics, 030106 microbiology, Lysine, Succinic Acid, Virulence, medicine.disease_cause, Tandem mass spectrometry, Biochemistry, Citric Acid, 03 medical and health sciences, Succinylation, Bacterial Proteins, medicine, [CHIM]Chemical Sciences, ComputingMilieux_MISCELLANEOUS, biology, Pseudomonas aeruginosa, Chemistry, Acetylation, General Chemistry, biology.organism_classification, 3. Good health, 030104 developmental biology, bacteria, [CHIM.OTHE]Chemical Sciences/Other, Protein Processing, Post-Translational, Bacteria
Abstract: Pseudomonas aeruginosa is a multi-drug-resistant human opportunistic pathogen largely involved in nosocomial infections. Unfortunately, effective antibacterial agents are lacking. Exploring its physiology at the post-translational modifications (PTMs) level may contribute to the renewal of combat tactics. Recently, lysine succinylation was discovered in bacteria and seems to be an interesting PTM. We present the first succinylome and acetylome of P. aeruginosa PA14 cultured in the presence of four different carbon sources using a 2D immunoaffinity approach coupled to nanoliquid chromatography tandem mass spectrometry. A total of 1520 succinylated (612 proteins) and 1102 acetylated (522 proteins) lysine residues were characterized. Citrate was the carbon source in which we identified the higher number of modified proteins. Interestingly, 622 lysine residues (312 proteins) were observed either acetylated or succinylated. Some of these proteins, were involved in virulence, adaptation, resistance, and so on. A label-free quantification points out the existence of different protein forms for a same protein (unmodified, succinylated or acetylated) and suggests different abundance as a function of the carbon sources. This work is a promising starting point for further investigations on the biological role of lysine succinylation in P. aeruginosa.
Published: 2018
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32. Proteomic profiling of lysine acetylation in Pseudomonas aeruginosa reveals the diversity of acetylated proteins

Author: Thierry Jouenne, Tassadit Ouidir, Pascal Cosette, and Julie Hardouin
Subjects: chemistry.chemical_classification, 0303 health sciences, 030306 microbiology, Proteomic Profiling, Pseudomonas aeruginosa, Lysine, Biology, medicine.disease_cause, Proteomics, Biochemistry, 03 medical and health sciences, Metabolic pathway, chemistry.chemical_compound, Enzyme, chemistry, Biosynthesis, Acetylation, medicine, Molecular Biology, 030304 developmental biology
Abstract: Protein lysine acetylation is a reversible and highly regulated post-translational modification with the well demonstrated physiological relevance in eukaryotes. Recently, its important role in the regulation of metabolic processes in bacteria was highlighted. Here, we reported the lysine acetylproteome of Pseudomonas aeruginosa using a proteomic approach. We identified 430 unique peptides corresponding to 320 acetylated proteins. In addition to the proteins involved in various metabolic pathways, several enzymes contributing to the lipopolysaccharides biosynthesis were characterized as acetylated. This data set illustrated the abundance and the diversity of acetylated lysine proteins in P. aeruginosa and opens opportunities to explore the role of the acetylation in the bacterial physiology.
Published: 2015
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33. Brain proteomic modifications associated to protective effect of grape extract in a murine model of obesity

Author: Safwen Kadri, Ferid Limam, Selima Smine, Pascal Cosette, Thierry Jouenne, Manuel Fréret, Julie Hardouin, Ezzedine Aouani, Mohamed Amri, Antoine Obry, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et biothérapies des maladies inflammatoires et autoimmunes, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Faculté des Sciences Mathématiques, Physiques et Naturelles de Tunis (FST), Université de Tunis El Manar (UTM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Faculté des Sciences de Bizerte [Université de Carthage], Université de Carthage - University of Carthage, Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: 0301 basic medicine, Proteomics, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Biophysics, Pharmacology, Biology, medicine.disease_cause, Diet, High-Fat, Biochemistry, Antioxidants, Mass Spectrometry, Analytical Chemistry, 03 medical and health sciences, Mice, 0302 clinical medicine, Pharmacotherapy, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Animals, Humans, Glycolysis, Calcium Signaling, Obesity, Molecular Biology, Calcium signaling, Grape Seed Extract, Brain, food and beverages, medicine.disease, 3. Good health, Rats, Oxidative Stress, 030104 developmental biology, Lipotoxicity, Gene Expression Regulation, Murine model, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress
Abstract: International audience; n recent years, the obesity epidemic has developed into a major health crisis worldwide. With current treatments limited to expensive, high-risk surgery and minimally efficacious pharmacotherapy, new therapeutic options are urgently needed to fight against this alarming trend. Though brain dysfunction has been studied linked to high fat diet (HFD) and grape seed and skin extract (GSSE) correction, the proteomic modifications linking the two effects on brain lipotoxicity are not well understood. To this end rats were exposed for 8 weeks to HFD treatment, to GSSE (500 mg/kg BW) and to binary mixture of HFD and GSSE to gain insight into the potential pathways altered with metabolic disease and the protection afforded by GSSE. Significant modifications of brain proteins were detected using mass spectrometry-based differential proteomics. These proteins were mainly related to oxidative stress, glycolysis and calcium signaling. Additionally, proteins involved in the cytoskeleton were also affected by HFD treatment. Interestingly, whether up- or down regulated protein abundances, GSSE corrected most of the disturbances of HFD treatment. These findings provide impetus for future therapeutic investigation on GSSE against other metabolic disorders.
Published: 2017
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34. Neuroprotective Activity of Grape Seed and Skin Extract Against Lithium Exposure Using Proteomic Research

Author: Olfa Khazri, Ferid Limam, Pascal Cosette, Abdelhafidh Khazri, Ezzeddine Aouani, Ali Mezni, Faculté des Sciences de Bizerte [Université de Carthage], Université de Carthage - University of Carthage, Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: 0301 basic medicine, Male, Proteomics, food.ingredient, Proteome, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Neuroscience (miscellaneous), Lithium, medicine.disease_cause, Neuroprotection, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, food, Phenols, Tandem Mass Spectrometry, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Animals, Protein Interaction Maps, Rats, Wistar, Grape Seed Extract, Proteomic research, Chemistry, Brain, Wistar rats, Oxidative Stress, 030104 developmental biology, Neuroprotective Agents, Neurology, Biochemistry, GSSE, Grape seed extract, Phosphoprotein, Toxicity, Signal transduction, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress, Chromatography, Liquid
Abstract: International audience; Lithium (Li) has raised scientific concern because it represents a serious problem threatening human health. This study aimed firstly at analyzing and potentially quantifying the impact of Li and grape seed and skin extract (GSSE) separately and, secondly, describing the possible neuroprotective activity of GSSE against Li toxicity. To this end, rats were exposed for 30 days to different Li concentrations (0, 2, and 100 mg/kg bw), to GSSE (4000 mg/kg bw), and to binary mixture of Li and GSSE. Liquid chromatography (HPLC–MS/MS) analysis used for GSSE showed that 15 phenolic compounds are present in the extract. Significant modifications of proteins were detected in the brain using proteomics research after treatment. Proteins were successfully identified by a linear ion trap–Orbitrap mass spectrometer. These proteins can be roughly related to oxidative stress, glycolysis, signaling pathway, and inflammation. Additionally, proteins involved in cell junction such as myosin, spectrin, tubulin, ERM-binding phosphoprotein, and dynein were also affected by Li exposure. Dose response was detected for most expressed proteins after Li treatment. In contrast, GSSE induced the expression and/or the stabilization of some proteins changed after Li treatment in the brain showing its neuroprotective activity. These data demonstrate that proteomic analysis is a powerful tool to provide valuable insights into mechanisms of toxicity of Li in the nervous system of Wistar rats. To our knowledge, this is the first evidence of using GSSE as neuroprotective model against Li toxicity. These findings provide impetus for future investigation on GSSE against other toxic chemicals.
Published: 2017
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35. Glioprotective effect of Ulva rigida extract against UVB cellular damages

Author: Mohamed Amri, Olfa Masmoudi, Ines Bourguiba, Annick Schaumann, Amine Ben Mlouka, Julie Hardouin, Thierry Jouenne, Amel Zehlila, Pascal Cosette, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Faculté des Sciences Mathématiques, Physiques et Naturelles de Tunis (FST), Université de Tunis El Manar (UTM), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, biology, Calmodulin, [SDV]Life Sciences [q-bio], Proteolytic enzymes, biology.organism_classification, Cellular viability, Ulva rigida, Lipid peroxidation, Superoxide dismutase, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, 0302 clinical medicine, Biochemistry, Algae, chemistry, Catalase, biology.protein, Agronomy and Crop Science, 030217 neurology & neurosurgery, ComputingMilieux_MISCELLANEOUS
Abstract: Natural molecules from different origins exhibit high therapeutic potential. Among them, molecules from marine algae are of particular interest. In the present study, we investigated the preventive effect of a protein extract (PE) of Ulva rigida against UVB-induced cellular damages. We demonstrated that a treatment of cortical astrocytes with 50 μg of PE induced a strong glioprotective effect and suppressed harmful effects of UVB radiations, increasing in particular cellular viability. In additional assays, this extract promoted the activity of catalase and superoxide dismutase and inhibited the production of stress markers, such as H 2 O 2 or lipid peroxidation. As expected, proteolytic digestion or heating treatment of algal extract inhibited this preventive effect, arguing for the predominant role of the protein fraction. Thereafter, proteomic investigations allowed to identify several proteins from the extract, among which calmodulin revealed to represent an important contributor to the observed protective activities.
Published: 2017
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36. Impaired vitreous composition and retinal pigment epithelium function in the FoxG1::LRP2 myopic mice

Author: Pascal Cosette, Sébastien Augustin, Sirine Ben-Yacoub, Antoine Obry, Manuel Simonutti, Géraldine Toutirais, Renata Kozyraki, Olivier Cases, Antoine Joseph, Annabel Christ, HAL-UPMC, Gestionnaire, Institut de la Vision, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et biothérapies des maladies inflammatoires et autoimmunes, Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Microscopie Electronique [IBPS] (IBPS-ME), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Max Delbrück Center for Molecular Medicine [Berlin] (MDC), Helmholtz-Gemeinschaft = Helmholtz Association, Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Polymères Biopolymères Surfaces (PBS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC), Acides nucléiques : dynamique, ciblage, et fonctions biologiques - Régulation et dynamique des génomes (ANDCFB), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Max Delbrück Center for Molecular Medicine [Berlin], and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN)
Subjects: 0301 basic medicine, genetic structures, Endocytic cycle, Mice, Transgenic, Nerve Tissue Proteins, Retinal Pigment Epithelium, Biology, Vitreous, Pathogenesis, Mice, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, low density lipoprotein receptor-related protein 2, lipoprotein receptor-related protein 2, High myopia, Myopia, medicine, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory Organs, Molecular Biology, Retinal pigment epithelium, ADP-Ribosylation Factors, Retinal detachment, Forkhead Transcription Factors, Anatomy, medicine.disease, LRP2, eye diseases, Endocytosis, Cell biology, Vitreous Body, Low Density Lipoprotein Receptor-Related Protein-2, 030104 developmental biology, medicine.anatomical_structure, chemistry, [SDV.MHEP.OS] Life Sciences [q-bio]/Human health and pathology/Sensory Organs, Low-density lipoprotein, 030221 ophthalmology & optometry, Molecular Medicine, low density, sense organs, Homeostasis, Retinopathy
Abstract: International audience; High myopia (HM) is one of the main causes of visual impairment and blindness all over the world and an unsolved medical problem. Persons with HM are predisposed to other eye pathologies such as retinal detachment, myopic retinopathy or glaucomatous optic neuropathy, complications that may at least partly result from the extensive liquefaction of the myopic vitreous gel. To identify the involvement of the liquid vitreous in the pathogenesis of HM we here analyzed the vitreous of the recently described highly myopic low density lipoprotein receptor-related protein 2 (Lrp2)-deficient eyes. Whereas the gel-like fraction was not apparently modified, the volume of the liquid vitreous fraction (LVF) was much higher in the myopic eyes. Biochemical and proteome analysis of the LVF revealed several modifications including a marked decrease of potassium, sodium and chloride, of proteins involved in ocular tissue homeostasis and repair as well as of ADP-ribosylation factor 4 (ARF4), a protein possibly involved in LRP2 trafficking. A small number of proteins, mainly comprising known LRP2 ligands or proteins of the inflammatory response, were over expressed in the mutants. Moreover the morphology of the LRP2-deficient retinal pigment epithelium (RPE) cells was affected and the expression of ARF4 as well as of proteins involved in degradative endocytosis was strongly reduced. Our results support the idea that impairment of the RPE structure and most likely endocytic function may contribute to the vitreal modifications and pathogenesis of HM.
Published: 2017
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37. The aliphatic amidase AmiE is involved in regulation of Pseudomonas aeruginosa virulence

Author: Pascal Cosette, Alain Dufour, Alexandre Crépin, Sylvie Chevalier, Pierre Cornelis, Julie Hardouin, Thibaut Rosay, Julien Vieillard, Perrine Bortolotti, Thomas Clamens, Joerg Overhage, Benoit Guery, Fergal O'Gara, Takfarinas Kentache, Anke Neidig, Teddy Grandjean, Marc G. J. Feuilloley, Marlies J. Mooij, Emeline Bouffartigues, Mélanie Hillion, Olivier Lesouhaitier, Laboratoire de Microbiologie Signaux et Microenvironnement (LMSM), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de Biotechnologie et Chimie Marines (LBCM), Université de Brest (UBO)-Université de Bretagne Sud (UBS)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS), Recherche translationelle relations hôte-pathogènes, Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Université Lille 2 - Faculté de Médecine, Karlsruhe Institute of Technology (KIT), University College Cork (UCC), Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Biologie et physiologie des états septiques, IFR114-Université de Lille, Droit et Santé, This work was supported by grants from the Communauté d’Agglomération d’Evreux, the Conseil Général de l′Eure, European Union (FEDER), the French Association 'Vaincre la Mucoviscidose' and the Partenariats Hubert Curien (PHC Ulysses). Financial support by the BioInterfaces (BIF) Program of the Karlsruhe Institute of Technology (KIT) in the Helmholtz Association is gratefully acknowledged., We wish to thank Magalie Barreau and Olivier Maillot for technical assistance. T. Clamens and T. Rosay are recipients of a doctoral fellowship from the French Ministry of Research (MRE)., Vriendenkring VUB, Microbiology, Université de Bretagne Sud (UBS)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Faculté de Médecine Henri Warembourg - Université de Lille, Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Bazire, Alexis
Subjects: Male, 0301 basic medicine, Virulence regulation, MESH: Pseudomonas Infections/microbiology, Proteome, health care facilities, manpower, and services, MESH: Dictyostelium/microbiology, MESH: Virulence, medicine.disease_cause, MESH: Quorum Sensing, Pilus, chemistry.chemical_compound, MESH: Caenorhabditis elegans/microbiology, MESH: Amidohydrolases/metabolism, AmiE overproduction, Dictyostelium, MESH: Animals, Lung, health care economics and organizations, MESH: Pseudomonas aeruginosa/enzymology, Multidisciplinary, Virulence, Quorum Sensing, MESH: Proteome, Pseudomonas aeruginosa, Female, Life sciences, biology, MESH: Virulence Factors, Virulence Factors, 030106 microbiology, Homoserine, MESH: Biofilms, Biology, Microbiology, Article, Amidohydrolases, Amidase, 03 medical and health sciences, Pyocyanin, MESH: Mice, Inbred C57BL, ddc:570, Journal Article, medicine, Animals, Pseudomonas Infections, cardiovascular diseases, Caenorhabditis elegans, MESH: Lung/microbiology, MESH: Pseudomonas aeruginosa/pathogenicity, Biofilm, Bacteriology, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Male, MESH: Pseudomonas Infections/enzymology, Mice, Inbred C57BL, Quorum sensing, chemistry, Biofilms, FOS: Biological sciences, Pseudomonas aeruginosa virulence, [SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Female
Abstract: We have previously shown that the eukaryotic C-type natriuretic peptide hormone (CNP) regulates Pseudomonas aeruginosa virulence and biofilm formation after binding on the AmiC sensor, triggering the amiE transcription. Herein, the involvement of the aliphatic amidase AmiE in P. aeruginosa virulence regulation has been investigated. The proteome analysis of an AmiE over-producing strain (AmiE+) revealed an expression change for 138 proteins, including some that are involved in motility, synthesis of quorum sensing compounds and virulence regulation. We observed that the AmiE+ strain produced less biofilm compared to the wild type, and over-produced rhamnolipids. In the same line, AmiE is involved in P. aeruginosa motilities (swarming and twitching) and production of the quorum sensing molecules N-acyl homoserine lactones and Pseudomonas Quinolone Signal (PQS). We observed that AmiE overproduction reduced levels of HCN and pyocyanin causing a decreased virulence in different hosts (i.e. Dictyostelium discoideum and Caenorhabditis elegans). This phenotype was further confirmed in a mouse model of acute lung infection, in which AmiE overproduction resulted in an almost fully virulence decrease. Taken together, our data suggest that, in addition to its role in bacterial secondary metabolism, AmiE is involved in P. aeruginosa virulence regulation by modulating pilus synthesis and cell-to-cell communication.
Published: 2017
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38. Potential of liquid-isoelectric-focusing protein fractionation to improve phosphoprotein characterization of Pseudomonas aeruginosa PA14

Author: Thierry Jouenne, Julie Hardouin, Pascal Cosette, Frédérique Jarnier, and Tassadit Ouidir
Subjects: Chromatography, Chemistry, Isoelectric focusing, Phosphoproteins, Proteomics, Tandem mass spectrometry, Biochemistry, Analytical Chemistry, Bacterial Proteins, Tandem Mass Spectrometry, Phosphoprotein, Pseudomonas aeruginosa, Proteome, Phosphorylation, Protein phosphorylation, Isoelectric Focusing, Tyrosine
Abstract: Protein phosphorylation on serine, threonine, and tyrosine is known to be involved in a wide variety of cellular processes and signal transduction in bacteria. Bacterial-proteome analysis is required to determine which proteins have been conditionally expressed and whether any post-translational modifications are present. One of the greatest challenges of proteome analysis is the fractionation of these complex protein mixtures to detect low-abundance phosphoproteins. Liquid-phase isoelectric focusing (IEF) is a promising analytical tool in proteomics, but as far as we are aware no work has studied the reproducibility of this approach. In this study, we investigated the phosphoproteome of Pseudomonas aeruginosa strain PA14. We first tested in-solution IEF protein fractionation, and then used this technique to fractionate the proteins in the complex mixture. Next, phosphopeptides were enriched with titanium dioxide and analyzed by high-resolution, high-accuracy liquid chromatography-mass spectrometry. With this approach, we succeeded in characterizing 73 unique phosphorylated peptides belonging to 63 proteins. Interestingly, we observed a higher percentage of modified tyrosine, revealing the importance of this phosphorylated residue in bacteria.
Published: 2014
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39. Proteomic regulation during Legionella pneumophila biofilm development: decrease of virulence factors and enhancement of response to oxidative stress

Author: Arbia Khemiri, Thierry Jouenne, Philippe Chan Chi Song, Pascal Cosette, Sandra Ahmed Lecheheb, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: Microbiology (medical), Proteases, Proteome, Virulence Factors, Legionella, [SDV]Life Sciences [q-bio], Virulence, Legionella pneumophila, Mass Spectrometry, Microbiology, Agar plate, 03 medical and health sciences, Electrophoresis, Gel, Two-Dimensional, Waste Management and Disposal, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Water Science and Technology, Analysis of Variance, Principal Component Analysis, 0303 health sciences, biology, 030306 microbiology, Public Health, Environmental and Occupational Health, Biofilm, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, Oxidative Stress, Infectious Diseases, Biofilms, Bacteria
Abstract: Legionella pneumophila (L. pneumophila) is a Gram-negative bacterium, which can be found worldwide in aquatic environments. It tends to persist because it is often protected within biofilms or amoebae. L. pneumophila biofilms have a major impact on water systems, making the understanding of the bacterial physiological adaptation in biofilms a fundamental step towards their eradication. In this study, we report for the first time the influence of the biofilm mode of growth on the proteome of L. pneumophila. We compared the protein patterns of microorganisms grown as suspensions, cultured as colonies on agar plates or recovered with biofilms formed on stainless steel coupons. Statistical analyses of the protein expression data set confirmed the biofilm phenotype specificity which had been previously observed. It also identified dozens of proteins whose abundance was modified in biofilms. Proteins corresponding to virulence factors (macrophage infectivity potentiator protein, secreted proteases) were largely repressed in adherent cells. In contrast, a peptidoglycan-associated lipoprotein (Lpg2043) and a peroxynitrite reductase (Lpg2965) were accumulated by biofilm cells. Remarkably, hypothetical proteins, that appear to be unique to the Legionella genus (Lpg0563, Lpg1111 and Lpg1809), were over-expressed by sessile bacteria.
Published: 2014
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40. Major remodeling of brain microvessels during neonatal period in the mouse: A proteomic and transcriptomic study

Author: Antoine Obry, Baptiste Porte, Thierry Lequerré, Soumeya Bekri, Yasmine Zerdoumi, Bruno J. Gonzalez, Céline Derambure, Philippe Leroux, Julie Hardouin, Pascal Cosette, Nicolas Dupré, Jean-Michel Flaman, Michèle Hauchecorne, Stéphane Marret, Endothélium microcirculatoire cérébral et lésions du système nerveux central au cours du développement (Néovasc), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Génomique et Médecine Personnalisée du Cancer et des Maladies Neuropsychiatriques (GPMCND), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Génétique du cancer et des maladies neuropsychiatriques (GMFC), Service de rhumatologie [CHU Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Physiopathologie et biothérapies des maladies inflammatoires et autoimmunes, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de biochimie générale [Rouen], Normandie Université (NU)-Centre hospitalier universitaire de Rouen, Maladies neurodéveloppementales et neurovasculaires (NeuroDiderot (UMR_S_1141 / U1141)), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Team 4 'NeoVasc' - INSERM U1245, Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Service de rhumatologie [Rouen], Normandie Université (NU)-Normandie Université (NU)-CHU Rouen, Institut de Physique du Globe de Paris (IPGP), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut national des sciences de l'Univers (INSU - CNRS)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Université de La Réunion (UR)-Centre National de la Recherche Scientifique (CNRS), Schulich School of Music & CIRMMT, and McGill University
Subjects: Male, Proteomics, 0301 basic medicine, Proteases, Proteome, Microarray, [SDV]Life Sciences [q-bio], Vascular Remodeling, Bioinformatics, Transcriptome, Andrology, Extracellular matrix, Mice, 03 medical and health sciences, 0302 clinical medicine, Subependymal zone, Animals, Medicine, ComputingMilieux_MISCELLANEOUS, Cerebral Hemorrhage, business.industry, Glutamate receptor, Brain, Gene Expression Regulation, Developmental, Original Articles, medicine.disease, Mice, Inbred C57BL, 030104 developmental biology, Intraventricular hemorrhage, Neurology, Microvessels, Forebrain, Female, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Neurology (clinical), Cardiology and Cardiovascular Medicine, business, 030217 neurology & neurosurgery
Abstract: Preterm infants born before 29 gestation weeks incur major risk of subependymal/intracerebral/intraventricular hemorrhage. In mice, neonate brain endothelial cells are more prone than adult cells to secrete proteases under glutamate challenge, and invalidation of the Serpine 1 gene is accompanied by high brain hemorrhage risk up to five days after birth. We hypothesized that the structural and functional states of microvessels might account for age-dependent vulnerability in mice up to five days after birth and might represent a pertinent paradigm to approach the hemorrhage risk window observed in extreme preterms. Mass spectrometry proteome analyses of forebrain microvessels at days 5, 10 and in adult mice revealed 899 proteins and 36 enriched pathways. Microarray transcriptomic study identified 5873 genes undergoing at least two-fold change between ages and 93 enriched pathways. Both approaches pointed towards extracellular matrix, cell adhesion and junction pathways, indicating delayed microvascular strengthening after P5. Furthermore, glutamate receptors, proteases and their inhibitors exhibited convergent evolutions towards excitatory aminoacid sensitivity and low proteolytic control likely accounting for vascular vulnerability in P5 mice. Thus, age vascular specificities must be considered in future therapeutic interventions in preterms. Data are available on ProteomeXchange (identifier PXD001718) and NCBI Gene-Expression-Omnibus repository (identification GSE67870).
Published: 2016
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41. Proteomics dedicated to biofilmology: What have we learned from a decade of research?

Author: Thierry Jouenne, Arbia Khemiri, Pascal Cosette, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: Proteomics, 0301 basic medicine, Microbiology (medical), Proteome, [SDV]Life Sciences [q-bio], 030106 microbiology, Immunology, General Medicine, Computational biology, Biology, Bioinformatics, 03 medical and health sciences, Gene Expression Regulation, Biofilms, Humans, Immunology and Allergy, ComputingMilieux_MISCELLANEOUS, Signal Transduction, Microbial Biofilms
Abstract: Advances in proteomics techniques over the past decade, closely integrated with genomic and physicochemical approach, have played a great role in developing knowledge of the biofilm lifestyle of bacteria. Despite bacterial proteome versatility, many studies have demonstrated the ability of proteomics approaches to elucidating the biofilm phenotype. Though these investigations have been largely used for biofilm studies in the last decades, they represent, however, a very low percentage of proteomics works performed up to now. Such approaches have offered new targets for combating microbial biofilms by providing a comprehensive quantitative and qualitative overview of their protein cell content. Herein, we summarized the state of the art in knowledge about biofilm physiology after one decade of proteomic analysis. In a second part, we highlighted missing research tracks for the next decade, emphasizing the emergence of posttranslational modifications in proteomic studies stemming from recent advances in mass spectrometry-based proteomics.
Published: 2016
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42. Putative use of a Bacillus subtilis L194 strain for biocontrol of Phoma medicaginis in Medicago truncatula seedlings

Author: Maria-Camino Urdaci, Thierry Jouenne, Ferid Limam, Jean Marie Schmitter, Imen Ben Slimene, Olfa Tabbene, Pascal Cosette, Naceur Djébali, Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)
Subjects: DNA, Bacterial, Antifungal Agents, Tunisia, [SDV]Life Sciences [q-bio], Molecular Sequence Data, Biological pest control, Bacillus subtilis, Microscopy, Atomic Force, DNA, Ribosomal, Microbiology, Conidium, Lipopeptides, 03 medical and health sciences, Ascomycota, Bacterial Proteins, RNA, Ribosomal, 16S, Antibiosis, Medicago truncatula, Botany, Pest Control, Biological, Molecular Biology, Soil Microbiology, ComputingMilieux_MISCELLANEOUS, Plant Diseases, 030304 developmental biology, 0303 health sciences, biology, Strain (chemistry), 030306 microbiology, Cell Membrane, fungi, Sequence Analysis, DNA, General Medicine, Spores, Fungal, 16S ribosomal RNA, biology.organism_classification, Bacterial Typing Techniques, Spore, Seedlings, Germination
Abstract: An antagonist L194 strain against Phoma medicaginis pathogenic fungi was isolated from Tunisian soil (vicinity of Tunis) and identified as Bacillus subtilis based on biochemical characteristics and partial 16S rDNA sequence. When cells were grown in a minimal medium for 24 h, spore culture supernatant exhibited 2-fold higher antifungal activity than vegetative cells. MALDI-TOF mass spectrometry analysis showed that L194 spores produced mainly iturins, surfactins and fengycins with long-chain fatty acids, and other not yet identified compounds. Both vegetative cells and spores of L194 efficiently reduced germination of P. medicaginis conidia. As revealed by atomic force microscopy, L194 spores modified conidia morphology from a regular to a deflated shape. Data suggest that lipopeptides interacted with the cytoplasmic membrane, causing pore formation. In vivo, L194 spores were highly protective against P. medicaginis by reducing disease symptoms and alleviating growth disturbance of Medicago truncatula seedlings. As a whole, the lipopeptide-producing L194 strain may be successfully used in biocontrol of plant diseases induced by phytopathogenic fungi such as P. medicaginis.
Published: 2012
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43. Anti-Candida effect of bacillomycin D-like lipopeptides from Bacillus subtilis B38

Author: Abdelhamid Gharbi, Imen Ben Slimene, Thierry Jouenne, Maria Luisa Mangoni, Leila Kalai, Olfa Tabbene, Ines Karkouch, Salem Elkahoui, Pascal Cosette, and Ferid Limam
Subjects: 0303 health sciences, Bacillaceae, biology, 030306 microbiology, Lipopeptide, Bacillus subtilis, biology.organism_classification, medicine.disease, Microbiology, Bacillales, Corpus albicans, Hemolysis, 3. Good health, 03 medical and health sciences, chemistry.chemical_compound, Bacillomycin, chemistry, Genetics, medicine, Candida albicans, Molecular Biology, 030304 developmental biology
Abstract: Bacillus subtilis B38, isolated from soil, showed antimicrobial activity against human pathogenic Candida albicans species. Specific PCR primers revealed the presence of the bamC gene, which is involved in the biosynthesis of bacillomycin D. Three anti-Candida compounds designated a(1) , a(2) and a(3) were purified from culture supernatant and identified using matrix-assisted laser desorption/ionization time-of-flight MS as analogues of bacillomycin D-like lipopeptides of 14, 15 and 16 carbon fatty acid long chains, respectively. The compound a(3) displayed the strongest fungicidal activity against pathogenic C. albicans strains. It was even more active than amphotericin B with a lethal concentration of 59.07 vs. 135.26 μM of the antimycotic drug against the pathogenic strain C. albicans sp. 311 isolated from finger nail. Only moderate or weak anti-Candida activity was recorded for a(1) and a(2) compounds. Furthermore, a(3) showed the highest hemolytic activity, reaching 50% hemolysis at 22.14 μM, whereas a(1) and a(2) displayed a limited hemolysis at 68.26 and 37.41 μM, respectively. These findings suggest that the acyl chain length of bacillomycin D-like lipopeptides plays a major role in hemolytic and antifungal activities.
Published: 2011
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44. Peroxiredoxin 2 is Involved in the Neuroprotective Effects of PACAP in Cultured Cerebellar Granule Neurons

Author: Alain Fournier, Pascal Cosette, David Vaudry, Magalie Bénard, Béatrice Botia, Aurélia Ravni, Bruno J. Gonzalez, Anthony Falluel-Morel, Damien Seyer, Hubert Vaudry, Thierry Jouenne, Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-CHU Rouen, Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), International Associated laboratory Samuel de Champlain, Institut National de la Recherche Scientifique [Québec] (INRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Institut Armand Frappier (INRS-IAF), Institut National de la Recherche Scientifique [Québec] (INRS)-Réseau International des Instituts Pasteur (RIIP), and This work was supported by INSERM (U413), the European Institute for Peptide Research (IFRMP23), the Institut de Recherches Scientifiques sur les Boissons (IREB), an Interreg 3A FEDER project, the ANR (06-JCJC-0071), and the Conseil Régional de Haute-Normandie. The work was conducted with the technical support of the proteomic facility of the IFRMP23 and the Platform for Cell Imaging of Haute-Normandie. BB was a recipient of a doctoral fellowship from the Société Française d’Alcoologie and a fellowship from the Fondation pour la Recherche Médicale. We thank Dr Mickaël Naassila for the quantification of ethanol level in blood samples.
Subjects: Small interfering RNA, [SDV]Life Sciences [q-bio], MESH: RNA, Small Interfering/genetics, MESH: Cerebellum/cytology, MESH: Amino Acid Sequence, 0302 clinical medicine, Cerebellum, MESH: Animals, RNA, Small Interfering, Cells, Cultured, MESH: Neurons/cytology, Neurons, 0303 health sciences, biology, medicine.diagnostic_test, Caspase 3, MESH: Pituitary Adenylate Cyclase-Activating Polypeptide/metabolism, General Medicine, respiratory system, 3. Good health, Neuroprotective Agents, MESH: Colforsin/metabolism, Pituitary Adenylate Cyclase-Activating Polypeptide, Tetradecanoylphorbol Acetate, hormones, hormone substitutes, and hormone antagonists, MESH: Cells, Cultured, Neurotrophin, endocrine system, MESH: Rats, Molecular Sequence Data, MESH: Neuroprotective Agents/metabolism, Adenylate kinase, Peroxiredoxin 2, Neuroprotection, MESH: Peroxiredoxins/metabolism, MESH: Ethanol/metabolism, 03 medical and health sciences, Cellular and Molecular Neuroscience, Western blot, MESH: Peroxiredoxins/genetics, medicine, Animals, Amino Acid Sequence, Rats, Wistar, Protein kinase C, 030304 developmental biology, MESH: Molecular Sequence Data, Ethanol, Colforsin, MESH: Neurons/metabolism, Peroxiredoxins, MESH: Rats, Wistar, Molecular biology, Rats, MESH: Tetradecanoylphorbol Acetate/metabolism, MESH: RNA, Small Interfering/metabolism, biology.protein, MESH: Pituitary Adenylate Cyclase-Activating Polypeptide/genetics, MESH: Caspase 3/metabolism, 030217 neurology & neurosurgery
Abstract: International audience; The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) is known to counteract in vitro the deleterious effects of toxic agents on cerebellar granule cell survival and differentiation. The potent antiapoptotic action of PACAP is mediated through inhibition of caspase-3 activity; however, additional proteins are likely involved and remain to be identified. Two-dimensional gel electrophoresis analysis coupled with mass spectrometry characterization led to the identification of a protein, peroxiredoxin 2, which was induced after a 6-h treatment with PACAP. Western blot analysis confirmed the regulation of peroxiredoxin 2 by PACAP and revealed that this protein is induced by both cyclic AMP and protein kinase C stimulators. Inhibition of peroxiredoxin 2 expression, using two distinct small-interfering RNAs (siRNAs), reduced the effect of PACAP on caspase-3 activity and cerebellar granule cell survival. Peroxiredoxin 2 expression was also induced in vivo and in vitro by ethanol. Although ethanol and PACAP exert opposite effects on caspase-3 activity, inhibition of peroxiredoxin 2 expression, using siRNAs, only reduced the ability of PACAP to prevent ethanol-induced caspase-3 activity. Taken together, these data indicate that peroxiredoxin 2 is probably involved in the neurotrophic effect of PACAP and suggest that this protein may have a therapeutic potential for the treatment of some neurodegenerative diseases
Published: 2008
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45. Presence inLegionella pneumophilaof a mammalian-like mitochondrial permeability transition pore?

Author: Arbia Khemiri, Pascal Cosette, and Thierry Jouenne
Subjects: Peptidylprolyl isomerase, Voltage-dependent anion channel, Multiprotein complex, Sequence Homology, Amino Acid, biology, Mitochondrial Permeability Transition Pore, Molecular Sequence Data, Computational Biology, Mitochondrion, biology.organism_classification, Mitochondrial Membrane Transport Proteins, Models, Biological, Microbiology, Legionella pneumophila, respiratory tract diseases, Cell biology, Mitochondrial membrane transport protein, Bacterial Proteins, Mitochondrial permeability transition pore, Genetics, biology.protein, Amino Acid Sequence, Molecular Biology, Peptide sequence
Abstract: The genome of Legionella pneumophila reveals the presence of a large number of genes coding for eukaryotic-like proteins. By using database searches and homology investigations, we identified three proteins in L. pneumophila whose sequences share similarities with that of eukaryotic polypeptides (lpg0211, lpg1974 and lpg1982). In eukaryotes, the corresponding proteins (PBR, peripheral benzodiazepine receptor; VDAC, voltage-dependant anion channel; and CypD, cyclophilin D) participate in the formation of the mammalian mitochondrial permeability transition pore (MPTP), a complex involved in cell apoptosis. Intriguingly, the presence of these proteins has never been reported in the same bacterium and constitutes, up to now, a unique feature of L. pneumophila. In Legionella, we hypothesize that these proteins are recruited in a multiprotein complex close to the MPTP that may regulate intracellular survival and/or proliferation.
Published: 2008
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46. Mise en évidence de l’expression parlegionella pneumophilade deux protéines susceptibles d’être impliquées dans la formation d’un complexe proche du système MPTP

Author: Arbia Khemiri, Thierry Jouenne, and Pascal Cosette
Subjects: Grande bretagne, Reino unido, Western europe, MPTP complex, Biology, Molecular biology, Royaume uni
Abstract: Legionella pneumophila est responsable de la maladie du legionnaire. On la trouve dans les eaux naturelles ou elle est capable de se multiplier au sein de protozoaires. Le sequencage du genome des trois souches de L. pneumophila : Paris (souche endemique en France), Lens (responsable des recentes epidemies dans le nord de la France) et Philadelphia (responsable de la premiere epidemie de legionellose) ont montre que cette bacterie possede un nombre tres important de genes codant des proteines homologues aux proteines eucaryotes. En utilisant des outils bioinformatiques, nous avons mis en evidence chez cette bacterie la presence de trois genes (tspO, omp32 et Icy) codant des polypeptides homologues a des proteines impliquees dans la formation d'un systeme proteique proche d'un pore de transition mitochondrial (MPTP). Dans la presente etude, nous analysons l'expression de deux de ces genes, omp32 et Icy, par une approche proteomique.
Published: 2008
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47. Suspension-cultured BY-2 tobacco cells produce and mature immunologically active house dust mite allergens

Author: Caroline Bonneau, Pascal Cosette, Olivia Tran Dinh, Véronique Gomord, François Dorlhac de Borne, Erika van Oort, David Lienard, Philippe Moingeon, Muriel Bardor, Ronald van Ree, Loïc Faye, Alain Didierlaurent, Laurence Van Overtvelt, Eric Wambre, Rene Delon, AII - Amsterdam institute for Infection and Immunity, APH - Amsterdam Public Health, and Experimental Immunology
Subjects: Allergy, medicine.medical_treatment, Cell Culture Techniques, Plant Science, medicine.disease_cause, law.invention, Allergen, law, Tobacco, medicine, Animals, House dust mite, biology, Immunogenicity, Pyroglyphidae, Immunotherapy, Allergens, Plants, Genetically Modified, biology.organism_classification, medicine.disease, Recombinant Proteins, respiratory tract diseases, Immunology, Recombinant DNA, Agronomy and Crop Science, Biotechnology
Abstract: The replacement of crude allergen extracts by selected allergens currently represents a major goal for the improvement of allergy diagnosis and immunotherapy. Indeed, the development of molecularly defined vaccines would facilitate both standardization and enhance batch-to-batch reproducibility as well as treatment specificity. In this study, we have investigated the potential of tobacco plant cells to produce biologically active forms of the two major allergens from the house dust mite. A detailed characterization of these plant-made allergens has shown similar proteolytic maturation and folding as well as comparable immunoreactivity to their natural counterparts. Altogether, our results exemplify that suspension-cultured BY-2 tobacco cells represent a low cost and environmentally safe expression system suitable to produce recombinant allergens from Dermatophagoides pteronyssinus under a form appropriate for diagnostic and therapeutic purposes.
Published: 2007
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48. Characterization of endophytic Bacillus strains from tomato plants (Lycopersicon esculentum) displaying antifungal activity against Botrytis cinerea Pers

Author: Rania Belaid, Christophe Rihouey, Ines Karkouch, Thierry Jouenne, Imen Ben Slimene, Marwa Bejaoui, Sana Azaeiz, Pascal Cosette, Ferid Limam, Asma Kefi, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), and Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie)
Subjects: Spectrometry, Mass, Electrospray Ionization, Antifungal Agents, food.ingredient, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, Physiology, Bacillus, Microbial Sensitivity Tests, Fungus, DNA, Ribosomal, Plant Roots, Applied Microbiology and Biotechnology, Lycopersicon, Microbiology, Lipopeptides, chemistry.chemical_compound, food, Solanum lycopersicum, Antibiosis, Botany, Endophytes, Pest Control, Biological, Mycelium, ComputingMilieux_MISCELLANEOUS, Plant Diseases, Botrytis cinerea, Botrytis, Base Sequence, Plant Stems, biology, fungi, food and beverages, General Medicine, biology.organism_classification, Plant Leaves, Biological Control Agents, chemistry, Peptides, Surfactin, Antagonism, Antimicrobial Cationic Peptides, Biotechnology
Abstract: Eighty endophytic bacteria were isolated from healthy tissues of roots, stems, leaves and fruits of tomato plants (Lycopersicon esculentum). Four strains, named BL1, BT5, BR8 and BF11 were selected for their antagonism against Botrytis cinerea, a phytopathogenic fungus responsible of gray mold in several important crops, with growth inhibitory activity ranging from 27 to 53%. Morphological, biochemical, and molecular parameters as 16S rDNA sequencing demonstrated that the selected bacterial strains were related to Bacillus species which are known to produce and secrete a lot of lipopeptides with strong inhibitory effect against pathogen mycelial growth. Electrospray mass spectrometry analysis showed that these strains produced heterogeneous mixture of antibiotics belonging to fengycin and surfactin for BL1 and BT5, to iturin and surfactin for BR8, to bacillomycin D, fengycin and surfactin for BF11. Furthermore, these bacteria exhibited biocontrol potential by reducing the disease severity when tested on detached leaflets. Based on their antifungal activity against Botrytis cinerea, these strains could be used for biological control of plant diseases.
Published: 2015
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49. Differential protein expression in the estuarine copepod Eurytemora affinis after diuron and alkylphenol exposures

Author: Céline, Boulangé-Lecomte, Béatrice, Rocher, Kévin, Cailleaud, Pascal, Cosette, Eléna, Legrand, David, Devreker, Hélène, Budzinski, Sami, Souissi, and Joëlle, Forget-Leray
Subjects: Copepoda, Phenols, Proteome, Diuron, Animals, Electrophoresis, Gel, Two-Dimensional, Energy Metabolism, Mass Spectrometry, Water Pollutants, Chemical
Abstract: Proteomics was used in the calanoid copepod Eurytemora affinis for screening of protein expression modifications induced by organic contaminants. The copepods were exposed in a continuous flow-through system for 86 h to environmentally relevant concentrations of contaminants representative of the pollution in the Seine Estuary (Haute-Normandie, France; diuron, 500 ng L(-1) ; alkylphenol mixture, 1000 ng L(-1) ). Proteome analysis of whole-body copepod extracts by 2-dimensional gel electrophoresis revealed that the contaminants induced modifications in protein expression, with the highest quantitative variations occurring after diuron exposure. Specifically, 88 and 41 proteins were differentially expressed after diuron and alkylphenol treatments, respectively. After mass spectrometry analysis, 51 (diuron exposure) and 15 (alkylphenol exposure) proteins were identified. The identified proteins were potentially related to energy metabolism, cell growth, nervous signal conductivity, excitotoxicity, oxidative stress response, and antioxidant defense. The data suggest a massive general disturbance of physiological functions of E. affinis after diuron exposure, whereas alkylphenols induced an alteration of a few targeted physiological functions. The protein expression signatures identified after contaminant exposure deserve further investigation in terms of the development of novel potential biomarkers for water quality assessment. Environ Toxicol Chem 2016;35:1860-1871. © 2015 SETAC.
Published: 2015

50. Determination of Multimodal Isotopic Distributions: The Case of a (15)N Labeled Protein Produced into Hairy Roots

Author: Patrice Lerouge, Michèle Boitel-Conti, Julie Hardouin, Carlos Afonso, Carole Plasson, Isabelle Ségalas-Milazzo, Vincent Tognetti, Laure Guilhaudis, Laurent Coquet, Marie Hubert-Roux, François Guerineau, Laurence Menu-Bouaouiche, Pascal Cosette, Jean-Pierre Ele Ekouna, Romain Trouillard, Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale (Glyco-MEV), Normandie Université (NU)-Normandie Université (NU), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Biologie des Plantes et Innovation - UR UPJV 3900 (BIOPI), Université de Picardie Jules Verne (UPJV), ANR-11-LABX-0029,SYNORG,Synthèse Organique : des molécules au vivant(2011), Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Picardie Jules Verne (UPJV)-Transfrontalière BioEcoAgro - UMR 1158 (BioEcoAgro), Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL)-Université d'Artois (UA)-Université de Liège-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), and Université catholique de Lille (UCL)-Université catholique de Lille (UCL)
Subjects: Population, Green Fluorescent Proteins, Proteomics, Mass spectrometry, 01 natural sciences, Plant Roots, Mass Spectrometry, Analytical Chemistry, Isotopic labeling, 03 medical and health sciences, Metabolomics, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, Humans, education, Fluxomics, 030304 developmental biology, 0303 health sciences, education.field_of_study, Chromatography, Isotope, Nitrogen Isotopes, Chemistry, 010401 analytical chemistry, Brassica rapa, Multimodal distribution, 0104 chemical sciences
Abstract: International audience; Isotopic labeling is widely used in various fields like proteomics, metabolomics, fluxomics, as well as in NMR structural studies, but it requires an efficient determination of the isotopic enrichment. Mass spectrometry is the method of choice for such analysis. However, when complex expression systems like hairy roots are used for production, multiple populations of labeled proteins may be obtained. If the isotopic incorporation determination is actually well-known for unimodal distributions, the multimodal distributions have scarcely been investigated. Actually, only a few approaches allow the determination of the different labeled population proportions from multimodal distributions. Furthermore, they cannot be used when the number of the populations and their respective isotope ratios are unknown. The present study implements a new strategy to measure the 15N labeled populations inside a multimodal distribution knowing only the peptide sequence and peak intensities from mass spectrometry analyses. Noteworthy, it could be applied to other elements, like carbon and hydrogen, and extended to a larger range of biomolecules.
Published: 2015
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