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323 results on '"Labesse G"'

11. Structural basis for chemically-induced homodimerization of a single domain antibody

Author

Lesne, J., Chang, H.J., De Visch, A., Paloni, M., Barthe, P., Guichou, J.F., Mayonove, P., Barducci, A., Labesse, G., Bonnet, J., Cohen-Gonsaud, M., Centre de Biochimie Structurale [Montpellier] (CBS), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Protein Conformation, [SDV]Life Sciences [q-bio], lcsh:R, lcsh:Medicine, Antibodies, Article, Structure-Activity Relationship, Models, Chemical, Caffeine, Humans, lcsh:Q, Immunoglobulin Domains, lcsh:Science, Dimerization
Abstract

International audience; Chemically-induced dimerization (CID) systems are essential tools to interrogate and control biological systems. AcVHH is a single domain antibody homo-dimerizing upon caffeine binding. AcVHH has a strong potential for clinical applications through caffeine-mediated in vivo control of therapeutic gene networks. Here we provide the structural basis for caffeine-induced homo-dimerization of acVHH.

Published
2019
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17. Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937

Author

Favey, S., Labesse, G., Vouille, V., and Boccara, M.

Subjects
Enterobacteriaceae -- Research, Genetic transcription -- Analysis, Cluster analysis -- Observations, Biological sciences
Abstract

The Flavohaemoglobin HmpX protein belongs to a family of flavohaemoproteins and it causes pathogenecity in plants that are contaminated with the Erwinia chrysanthemi strain 3937 enterobacterium. Mutated HmpX has reduced toxicity due to a lack of oxygen in plant intercellular fluid, as HmpX requires oxygen to flourish. Hydrophobic cluster analysis shows that HmpX has two functional regions, a haemoglobin domain in its N-terminal part and a flavin reductase domain in its C-terminal part. The induction of hmpX transcription in coculture with tobacco cells is found using gas fusion in hmpX.

Published
1995

29. The Leishmania nicotinamidase is essential for NAD(+) production and parasite proliferation

Author

Gazanion, Elodie, Garcia, Deborah, Silvestre, R., Gérard, C., Guichou, J. F., Labesse, G., Seveno, Martial, Cordeiro-Da-Silva, A., Ouaissi, A., Sereno, Denis, and Vergnes, Baptiste

Subjects
parasitic diseases
Abstract

NAD(+) is a central cofactor that plays important roles in cellular metabolism and energy production in all living cells. Genomics-based reconstruction of NAD(+) metabolism revealed that Leishmania protozoan parasites are NAD(+) auxotrophs. Consequently, these parasites require assimilating NAD(+) precursors (nicotinamide, nicotinic acid, nicotinamide riboside) from their host environment to synthesize NAD(+) by a salvage pathway. Nicotinamidase is a key enzyme of this salvage pathway that catalyses conversion of nicotinamide (NAm) to nicotinic acid (Na), and that is absent in higher eukaryotes. We present here the biochemical and functional characterizations of the Leishmania infantum nicotinamidase (LiPNC1). Generation of Lipnc1 null mutants leads to a decrease in NAD(+) content, associated with a metabolic shutdown-like phenotype with an extensive lag phase of growth. Both phenotypes could be rescued by an add-back construct or by addition of exogenous Na. In addition, Lipnc1 null mutants were unable to establish a sustained infection in a murine experimental model. Altogether, these results illustrate that NAD(+) homeostasis is a fundamental component of Leishmania biology and virulence, and that NAm constitutes its main NAD(+) source in the mammalian host. The crystal structure of LiPNC1 we solved allows now the design of rational inhibitors against this new promising therapeutic target.

Published
2011

37. Inhibition of 7,8-diaminopelargonic acid aminotransferase from Mycobacterium tuberculosis by chiral and achiral anologs of its substrate: biological implications

Author

Mann, S., Colliandre, L., Labesse, G., Ploux, O., Laboratoire Charles Friedel, Université Pierre et Marie Curie - Paris 6 (UPMC)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2009

44. Mutations in IMPG1 Cause Vitelliform Macular Dystrophies

Author

Manes, G., Meunier, I., Avila-Fernandez, A., Banfi, S., Meur, G. Le, Zanlonghi, X., Corton, M., Simonelli, F., Brabet, P., Labesse, G., Audo, I., Mohand-Said, S., Zeitz, C., Sahel, J.A., Weber, M., Dollfus, H., Dhaenens, C.M., Allorge, D., Baere, E. de, Koenekoop, R.K., Kohl, S., Cremers, F.P.M., Hollyfield, J.G., Senechal, A., Hebrard, M., Bocquet, B., Garcia, C.A., Hamel, C.P., Manes, G., Meunier, I., Avila-Fernandez, A., Banfi, S., Meur, G. Le, Zanlonghi, X., Corton, M., Simonelli, F., Brabet, P., Labesse, G., Audo, I., Mohand-Said, S., Zeitz, C., Sahel, J.A., Weber, M., Dollfus, H., Dhaenens, C.M., Allorge, D., Baere, E. de, Koenekoop, R.K., Kohl, S., Cremers, F.P.M., Hollyfield, J.G., Senechal, A., Hebrard, M., Bocquet, B., Garcia, C.A., and Hamel, C.P.

Abstract

Item does not contain fulltext, Vitelliform macular dystrophies (VMD) are inherited retinal dystrophies characterized by yellow, round deposits visible upon fundus examination and encountered in individuals with juvenile Best macular dystrophy (BMD) or adult-onset vitelliform macular dystrophy (AVMD). Although many BMD and some AVMD cases harbor mutations in BEST1 or PRPH2, the underlying genetic cause remains unknown for many affected individuals. In a large family with autosomal-dominant VMD, gene mapping and whole-exome sequencing led to the identification of a c.713T>G (p.Leu238Arg) IMPG1 mutation, which was subsequently found in two other families with autosomal-dominant VMD and the same phenotype. IMPG1 encodes the SPACR protein, a component of the rod and cone photoreceptor extracellular matrix domains. Structural modeling indicates that the p.Leu238Arg substitution destabilizes the conserved SEA1 domain of SPACR. Screening of 144 probands who had various forms of macular dystrophy revealed three other IMPG1 mutations. Two individuals from one family affected by autosomal-recessive VMD were homozygous for the splice-site mutation c.807+1G>T, and two from another family were compound heterozygous for the mutations c.461T>C (p.Leu154Pro) and c.1519C>T (p.Arg507( *)). Most cases had a normal or moderately decreased electrooculogram Arden ratio. We conclude that IMPG1 mutations cause both autosomal-dominant and -recessive forms of VMD, thus indicating that impairment of the interphotoreceptor matrix might be a general cause of VMD.

Published
2013

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