References of "Galleni, Moreno"
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See detailSPECIFICITY OF CLASS I TAGATOSE 1,6-BISPHOSPHATE ALDOLASE ENHANCED TOWARD TAGATOSE 1,6-BISPHOPHATE
Freichels, Régine ULiege; Delmarcelle, Michaël ULiege; Colarusso, Andrea et al

Poster (2015, July)

Class I tagatose 1,6-bisphosphate aldolase catalyzes the reversible condensation of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate to produce four D-ketohexoses 1,6-bisphosphate: D-tagatose 1,6 ... [more ▼]

Class I tagatose 1,6-bisphosphate aldolase catalyzes the reversible condensation of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate to produce four D-ketohexoses 1,6-bisphosphate: D-tagatose 1,6-bisphosphate, D-fructose 1,6-bisphosphate, D-psicose 1,6-bisphosphate and D-sorbose 1,6-bisphosphate. These four sugars are diastereoisomers and differs from each other in their stereochemistry at carbons 3 and 4. The structure determination of three class I tagatose 1,6-bisphosphate aldolases has afforded new insight into their catalytic mechanism as well as their evolution. However, the determinant(s) that allow(s) the enzyme to be so unspecific at carbon 4 have remains unknown. The aim of this project is focused on the characterization of the structural features of tagatose 1,6-bisphosphate aldolases that determine the specificity of the enzyme towards tagatose versus fructose 1,6-bisphosphate (carbon C4). [less ▲]

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See detailDevelopment of recombinant stable house dust mite allergen Der p 3 molecules for component resolved diagnosis and specific immunotherapy
Bouaziz, Ahlem ULiege; Galleni, Moreno ULiege; Louis, Renaud ULiege

in Clinical and Experimental Allergy (2015), 45

Abstract BACKGROUND: The allergen Der p 3 is underrepresented in house dust mite (HDM) extracts probably due to autolysis. Recombinant stable molecule of the allergen is thus needed to improve the ... [more ▼]

Abstract BACKGROUND: The allergen Der p 3 is underrepresented in house dust mite (HDM) extracts probably due to autolysis. Recombinant stable molecule of the allergen is thus needed to improve the diagnosis of allergy and the safety and efficacy of immunotherapy. OBJECTIVE: The current study reports the immunological characterization of two recombinant molecules of the HDM allergen Der p 3 as useful tools for diagnosis and immunotherapy. METHODS: Recombinant mature (rDer p 3) and immature (proDer p 3) Der p 3 and their corresponding S196A mutants were produced in Pichia pastoris and purified. The stability, IgE-binding capacity and allergenicity of the different proteins were analysed and compared with those of the major mite allergen Der p 1 used as a reference. Additionally, the immunogenicity of the different allergens was evaluated in a murine model of Der p 3 sensitization. RESULTS: Compared to the IgE reactivity to recombinant and natural Der p 3 (nDer p 3), the mean IgE binding of patient's sera to rDer p 3-S196A (50%) was higher. The poorly binding to nDer p 3 or rDer p 3 was due to autolysis of the allergen. Contrary to Der p 3, proDer p 3 displayed very weak IgE reactivity, as measured by sandwich ELISA and competitive inhibition, rat basophil leukaemia degranulation and human basophil activation assays. Moreover, proDer p 3 induced a TH 1-biased immune response that prevented allergic response in mice but retained Der p 3-specific T-cell reactivity. CONCLUSION: rDer p 3-S196A should be used for the diagnosis of HDM allergy elicited by Der p 3, and proDer p 3 may represent a hypoallergen of Der p 3. [less ▲]

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See detailRésistance aux antibiotiques : le retour à l’ère prébiotique ?
Galleni, Moreno ULiege; Kerff, Frédéric ULiege; Rigali, Sébastien ULiege

Conference (2015, February 05)

Aujourd’hui, la résistance des bactéries aux antibiotiques relève d'une préoccupation croissante dans le domaine de la santé publique et s'impose plus que jamais comme une priorité. Ce problème a un coût ... [more ▼]

Aujourd’hui, la résistance des bactéries aux antibiotiques relève d'une préoccupation croissante dans le domaine de la santé publique et s'impose plus que jamais comme une priorité. Ce problème a un coût, sociétal et économique en Europe: 25.000 décès annuels par septicémie et 1,5 milliard d’euros d’augmentation du coût des traitements. Bien que le besoin de nouveaux agents antibactériens en milieu clinique est urgent, seules deux nouvelles classes d’antibiotiques ont pu être proposées durant ces 30 dernières années. En effet, la découverte et le développement de nouveaux antibiotiques posent des défis scientifiques, cliniques et financiers importants. [less ▲]

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See detailGeneration of a soluble recombinant trimeric form of bovine CD40L and its potential use as a vaccine adjuvant in cows
Pujol, Julien ULiege; Bouillenne, Fabrice ULiege; Farnir, Frédéric ULiege et al

in Veterinary immunology and immunopathology (2015), 168(1), 1-13

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See detailStructural and Kinetic Insights into the "Ceftazidimase" Behavior of the Extended-Spectrum beta-Lactamase CTX-M-96.
Ghiglione, Barbara; Rodriguez, Maria Margarita; Herman, Raphaël ULiege et al

in Biochemistry (2015), 54(32), 5072-82

Diversification of the CTX-M beta-lactamases led to the emergence of variants responsible for decreased susceptibility to ceftazidime, like the Asp240Gly-harboring "ceftazidimases". We solved the ... [more ▼]

Diversification of the CTX-M beta-lactamases led to the emergence of variants responsible for decreased susceptibility to ceftazidime, like the Asp240Gly-harboring "ceftazidimases". We solved the crystallographic structure of the Asp240Gly variant CTX-M-96 at 1.2 A and evaluated the role of Asp240 in the activity toward oxyimino-cephalosporins through simulated models and kinetics. There seem to be subtle changes in the conformation of the active site cavity of CTX-M-96, compared to enzyme variants harboring the Asp240, and these small rearrangements could be due to localized shifts in the environment of the beta3 strand. According to the crystallographic evidence, CTX-M-96 presents a "compact" active site, which in spite of its reduced cavity seems to allow the proper interaction with oxyimino-cephalosporins, as suggested by simulated models. The term "ceftazidimases" that is currently applied for the Asp240Gly-harboring CTX-M variants should be used carefully. Structural differences between CTX-M harboring the Asp240Gly mutation (and also probably others like those at Pro167) do not seem to be conclusive to determine the "ceftazidimase" behavior observed in vivo, which is in turn partially supported by the mild improvement in the catalytic efficiency toward ceftazidime by CTX-M-96 and similar enzymes, compared to "parental" Asp240-harboring variants. In addition, it is observed that alterations in OmpF expression could act synergistically with CTX-M-96 for yielding clinical resistance toward ceftazidime. We therefore propose that the observed resistance in vivo is due to the sum of synergic mechanisms, and the term "cefotaximases associated with ceftazidime resistance" could be conveniently used to describe CTX-M harboring the Asp240Gly substitution. [less ▲]

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See detailKinetics of the interaction between avibactam and the CHE-1 class C beta-lactamase
Fernea, Adriana; Galleni, Moreno ULiege; Frère, Jean-Marie ULiege

in Journal of Antimicrobial Chemotherapy (2015), 70(3), 951--953

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See detailStructural and functional analysis of the HMA4 protein
Lekeux, Gilles ULiege; Laurent, Clémentine ULiege; Damblon, Christian ULiege et al

Poster (2014, September 09)

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See detailSynthesis of N-fluoroalkyl-tryptophan and study of their biological activity as potential substrates for indoleamine 2,3-dioxygenase
Henrottin, Jean ULiege; Zervosen, Astrid ULiege; Lemaire, Christian ULiege et al

Poster (2014, June)

Indoleamine 2,3-dioxygenase (rhIDO) is an enzyme mainly expressed in brain and tumor cells and catalyzing the oxidative cleavage of the indole ring of L-tryptophan through the kynurenine pathway ... [more ▼]

Indoleamine 2,3-dioxygenase (rhIDO) is an enzyme mainly expressed in brain and tumor cells and catalyzing the oxidative cleavage of the indole ring of L-tryptophan through the kynurenine pathway. Furthermore this enzyme could be responsible for the eventual suppression of immune responses by blocking locally T-lymphocyte proliferation. The syntheses of 1-(2-fluoroethyl)-tryptophan (1-[19F]FETrp) and 1-((1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl)methyl)-tryptophan, two N-fluoroalkylated tryptophan derivatives, are described here. In vitro enzymatic assays with these two new potential substrates of rhIDO show that 1-[19F]FETrp is a good and specific substrate of hIDO. [less ▲]

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See detailHow to build a biological linker dedicated to the engineering of novel drug delivery systems
Crasson, Oscar ULiege; Galleni, Moreno ULiege; Parente, Raffaella et al

Poster (2014, May 15)

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See detailDevelopment of recombinant stable house dust mite allergen Der p 3 molecules for component-resolved diagnosis and specific immunotherapy.
Bouaziz, Ahlem ULiege; Walgraffe, David; Bouillot, Celine et al

in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology (2014)

BACKGROUND: The allergen Der p 3 is underrepresented in house dust mite (HDM) extracts probably due to autolysis. Recombinant stable molecule of the allergen is thus needed to improve the diagnosis of ... [more ▼]

BACKGROUND: The allergen Der p 3 is underrepresented in house dust mite (HDM) extracts probably due to autolysis. Recombinant stable molecule of the allergen is thus needed to improve the diagnosis of allergy and the safety and efficacy of immunotherapy. OBJECTIVE: The current study reports the immunological characterization of two recombinant molecules of the HDM allergen Der p 3 as useful tools for diagnosis and immunotherapy. METHODS: Recombinant mature (rDer p 3) and immature (proDer p 3) Der p 3 and their corresponding S196A mutants were produced in Pichia pastoris and purified. The stability, IgE-binding capacity and allergenicity of the different proteins were analyzed and compared with those of the major mite allergen Der p 1 used as a reference. Additionally, the immunogenicity of the different allergens was evaluated in a murine model of Der p 3 sensitization. RESULTS: Compared to the IgE reactivity to recombinant and natural Der p 3 (nDer p 3), the mean IgE binding of patient's sera to rDer p 3-S196A (50 %) was higher. The poorly binding to nDer p 3 or rDer p 3 was due to autolysis of the allergen. Contrary to Der p 3, proDer p 3 displayed very weak IgE reactivity, as measured by sandwich ELISA and competitive inhibition, RBL degranulation and human basophil activation assays. Moreover, proDer p 3 induced a TH 1-biased immune response that prevented an allergic response in mice but retained Der p 3-specific T cell reactivity. CONCLUSION: rDer p 3-S196A should be used for the diagnosis of HDM allergy elicited by Der p 3, and proDer p 3 may represent a hypoallergen of Der p 3. This article is protected by copyright. All rights reserved. [less ▲]

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See detailOrchestration of an uncommon maturation cascade of the house dust mite protease allergen quartet.
Dumez, Marie-Eve; Herman, Julie; Campizi, Vincenzo et al

in Frontiers in immunology (2014), 5

In more than 20% of the world population, sensitization to house dust mite allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto ... [more ▼]

In more than 20% of the world population, sensitization to house dust mite allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, group 1 is cysteine proteases belonging to the papain-like family whereas groups 3, 6, and 9 are serine proteases displaying trypsin, chymotrypsin, and collagenolytic activities, respectively. While these proteases are more likely to be involved in the mite digestive system, they also play critical roles in the initiation and in the chronicity of the allergic response notably through the activation of innate immune pathways. All these allergenic proteases are expressed in mite as inactive precursor form. Until recently, the exact mechanisms of their maturation into active proteases remained to be fully elucidated. Recent breakthroughs in the understanding of the activation mechanisms of mite allergenic protease precursors have highlighted an uncommon and unique maturation pathway orchestrated by group 1 proteases that tightly regulates the proteolytic activities of groups 1, 3, 6, and 9 through complex intra- or inter-molecular mechanisms. This review presents and discusses the currently available knowledge of the activation mechanisms of group 1, 3, 6, and 9 allergens of Dermatophagoides pteronyssinus laying special emphasis on their localization, regulation, and interconnection. [less ▲]

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See detailStudy of a Natural Mutant SHV-Type beta-Lactamase, SHV-104, from Klebsiella pneumoniae
Achour, Nahed Ben; Belhadj, Omrane; Galleni, Moreno ULiege et al

in International journal of microbiology (2014), 2014

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See detailCrystal Structure of the Extended-Spectrum β -Lactamase PER-2 and Insights into the Role of Specific Residues in the Interaction with β -Lactams and β -Lactamase Inhibitors
Ruggiero, Melina; Kerff, Frédéric ULiege; Herman, Raphaël ULiege et al

in Antimicrobial Agents and Chemotherapy (2014), 58(10), 5994-6002

PER-2 belongs to a small (7 members to date) group of extended-spectrum beta-lactamases. It has 88% amino acid identity with PER-1 and both display high catalytic efficiencies toward most beta-lactams. In ... [more ▼]

PER-2 belongs to a small (7 members to date) group of extended-spectrum beta-lactamases. It has 88% amino acid identity with PER-1 and both display high catalytic efficiencies toward most beta-lactams. In this study, we determined the X-ray structure of PER-2 at 2.20 A and evaluated the possible role of several residues in the structure and activity toward beta-lactams and mechanism-based inhibitors. PER-2 is defined by the presence of a singular trans bond between residues 166 to 167, which generates an inverted Omega loop, an expanded fold of this domain that results in a wide active site cavity that allows for efficient hydrolysis of antibiotics like the oxyimino-cephalosporins, and a series of exclusive interactions between residues not frequently involved in the stabilization of the active site in other class A beta-lactamases. PER beta-lactamases might be included within a cluster of evolutionarily related enzymes harboring the conserved residues Asp136 and Asn179. Other signature residues that define these enzymes seem to be Gln69, Arg220, Thr237, and probably Arg/Lys240A ("A" indicates an insertion according to Ambler's scheme for residue numbering in PER beta-lactamases), with structurally important roles in the stabilization of the active site and proper orientation of catalytic water molecules, among others. We propose, supported by simulated models of PER-2 in combination with different beta-lactams, the presence of a hydrogen-bond network connecting Ser70-Gln69-water-Thr237-Arg220 that might be important for the proper activity and inhibition of the enzyme. Therefore, we expect that mutations occurring in these positions will have impacts on the overall hydrolytic behavior. [less ▲]

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