VASSEUR Jean-Jacques
Fonction : Directeur Adjoint
Thème de Recherche: Oligonucléotides Modifiés (responsable de)
jean-jacques.vasseur
umontpellier.fr
0448792048
Bureau: N1H02, Etg: 1, Bât: Balard - Site : Pôle Chimie Balard Recherche
Domaines de Recherche: - Sciences du Vivant/Médecine humaine et pathologie
- Chimie/Matériaux
- Chimie/Autre
- Sciences du Vivant/Microbiologie et Parasitologie/Virologie
- Sciences du Vivant/Biochimie, Biologie Moléculaire/Biochimie
- Sciences du Vivant/Immunologie/Immunité innée
- Sciences du Vivant/Biochimie, Biologie Moléculaire/Biologie structurale
- Sciences du Vivant/Biotechnologies
- Sciences du Vivant/Bio-Informatique, Biologie Systémique
- Sciences du Vivant/Microbiologie et Parasitologie/Bactériologie
- Sciences du Vivant/Neurosciences/Neurobiologie
- Sciences du Vivant/Sciences pharmaceutiques/Pharmacologie
- Sciences du Vivant/Médecine humaine et pathologie/Maladies émergentes
- Sciences du Vivant/Médecine humaine et pathologie/Maladies infectieuses
- Chimie/Chimie organique
- Chimie
- Sciences de l'ingénieur
- Sciences de l'ingénieur/ photonique
- Sciences de l'ingénieur/Microélectronique
- Sciences de l'ingénieur/Matériaux
- Chimie/Chimie analytique
- Sciences du Vivant/Biochimie, Biologie Moléculaire
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Dernieres productions scientifiques :
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An Innovative Multiplexed And Flexible Molecular Approach For The Differential Detection Of Arboviruses
Auteur(s): Leon Fanny, Meyer A., Reynier Robin, Blanc Emilie, Bruyère-Ostells Lilian, Bres Jean-Charles, Simonin Yannick, Salinas Sara, Gallian Pierre, Leparc-Goffart Isabelle, Biron Antoine, Dupont-Rouzeyrol Myrielle, Morvan F., Vasseur J.-J., Foulongne Vincent, Van De Perre Philippe, Cantaloube Jean-François, Fournier-Wirth Chantal
(Article) Publié:
The Journal Of Molecular Diagnostics/15251578, vol. p. (2018)
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The anti-adhesive effect of glycoclusters on Pseudomonas aeruginosa bacteria adhesion to epithelial cells studied by AFM single cell force spectroscopy
Auteur(s): Zuttion Francesca, Ligeour C., Vidal Olivier, Wälte Mike, Morvan F., Vidal Sébastien, Vasseur J.-J., Chevolot Yann, Phaner-Goutorbe Magali, Schillers Hermann
(Article) Publié:
Nanoscale, vol. 10 p.12771 - 12778 (2018)
Ref HAL: hal-01849823_v1
DOI: 10.1039/c8nr03285h
Résumé: The human opportunistic pathogen Pseudomonas aeruginosa (PA) is responsible for chronic infections of the respiratory epithelium in cystic fibrosis patients. PA takes advantage of an arsenal of virulence factors to infect and colonize human lungs. Among them, the lectin LecA favours epithelium invasion by interacting with host cell globotriaosylceramide (Gb3). A new therapeutic approach is based on the development of synthetic multivalent molecules (glycoclusters) targeting LecA with a higher affinity than its natural ligand. Atomic force microscopy-single cell force spectroscopy has been used to study the effect of glycoclusters on the bacteria–cell interaction. Glycoclusters have been shown to affect the detachment work and detachment force of the bacteria–cell interaction. The specificity and the efficiency of the glycocluster in targeting the lectin and destabilizing the PA–epithelial cell adhesion are demonstrated and discussed.
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Synthesis and screening of Oligisaccharides Clusters Targeting Lectins from Pseudomonas aeruginosa
Auteur(s): Dupin Lucie, Noel M., Bastide Ludovic, Meyer A., BONNET S., COTTIN C., Randriantsoa M., Gehin Thomas, Souteyrand Eliane, Vasseur J.-J., vidal olivier, Chevolot Yann, Vergoten G., Morvan F., DARBLADE B.
(Affiches/Poster)
Eurocarb 2017 (Barcelone, ES), 2017-07-02
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Cibler la lectine soluble Leca de Pseudomonas aeruginosa: une approche Drug-discovery sur DDI-microarray
Auteur(s): Dupin Lucie, Meyer A., Phaner-Goutorbe Magali, Morvan F., Laurenceau Emmanuelle, Vergoten G., Vasseur J.-J., Casoni F., Ligeour C., DARBLADE B., Vidal Olivier, Gehin Thomas, Chevolot Yann
(Affiches/Poster)
2ème Journées plénières du GDR B2I (Bordeaux, FR), 2017-06-28
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Binding of the Methyl Donor S -Adenosyl-l-Methionine to Middle East Respiratory Syndrome Coronavirus 2′- O -Methyltransferase nsp16 Promotes Recruitment of the Allosteric Activator nsp10
Auteur(s): Aouadi Wahiba, Blanjoie A., Vasseur J.-J., Debart F., Canard Bruno, Decroly Etienne
(Article) Publié:
Journal Of Virology, vol. 91 p.1103-1119 (2017)
Ref HAL: hal-01802788_v1
PMID 28031370
DOI: 10.1128/JVI.02217-16
Résumé: The Middle East respiratory syndrome coronavirus (MERS-CoV) nonstructural protein 16 (nsp16) is an S-adenosyl-l-methionine (SAM)-dependent 2'-O-methyltransferase (2'-O-MTase) that is thought to methylate the ribose 2'-OH of the first transcribed nucleotide (N1) of viral RNA cap structures. This 2'-O-MTase activity is regulated by nsp10. The 2'-O methylation prevents virus detection by cell innate immunity mechanisms and viral translation inhibition by the interferon-stimulated IFIT-1 protein. To unravel the regulation of nsp10/nsp16 2'-O-MTase activity, we used purified MERS-CoV nsp16 and nsp10. First, we showed that nsp16 recruited N7-methylated capped RNA and SAM. The SAM binding promotes the assembly of the enzymatically active nsp10/nsp16 complex that converted 7mGpppG (cap-0) into 7mGpppG2'Om (cap-1) RNA by 2'-OH methylation of N1 in a SAM-dependent manner. The subsequent release of SAH speeds up nsp10/nsp16 dissociation that stimulates the reaction turnover. Alanine mutagenesis and RNA binding assays allowed the identification of the nsp16 residues involved in RNA recognition forming the RNA binding groove (K46, K170, E203, D133, R38, Y47, and Y181) and the cap-0 binding site (Y30, Y132, and H174). Finally, we found that nsp10/nsp16 2'-O-MTase activity is sensitive to known MTase inhibitors, such as sinefungin and cap analogues. This characterization of the MERS-CoV 2'-O-MTase is a preliminary step toward the development of molecules to inhibit cap 2'-O methylation and to restore the host antiviral response.IMPORTANCE: MERS-CoV codes for a cap 2'-O-methyltransferase that converts cap-0 into cap-1 structure in order to prevent virus detection by cell innate immunity mechanisms. We report the biochemical properties of MERS-CoV 2'O-methyltransferase, which is stimulated by nsp10 acting as an allosteric activator of the nsp16 2'-O-methyltransferase possibly through enhanced RNA binding affinity. In addition, we show that SAM promotes the formation of the active nsp10/nsp16 complex. Conversely, after cap methylation, the reaction turnover is speeded up by cap-1 RNA release and nsp10/nsp16 complex dissociation, at the low intracellular SAH concentration. These results suggest that SAM/SAH balance is a regulator of the 2'-O-methyltransferase activity and raises the possibility that SAH hydrolase inhibitors might interfere with CoV replication cycle. The enzymatic and RNA binding assays developed in this work were also used to identify nsp16 residues involved in cap-0 RNA recognition and to understand the action mode of known methyltransferase inhibitors.
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