Publications of Loïc Quinton
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See detailVenomics approach reveals a high proportion of Lactrodectus-like toxins in Steatoda nobilis venom - First link to post-bite symptomology
Dunbar, John; Fort, Antoine; Redureau, Damien ULiege et al

Poster (2020, September)

The Noble false widow spider Steatoda nobilis has expanded its range globally and may represent a potential threat to native ecosystems and public health. Envenomations can result in local and systemic ... [more ▼]

The Noble false widow spider Steatoda nobilis has expanded its range globally and may represent a potential threat to native ecosystems and public health. Envenomations can result in local and systemic neurotoxic symptoms, similar to true black widows (genus Latrodectus). We used transcriptomic and proteomic cutting-edge approaches to deeply characterise S. nobilis venom. Among the toxins, the most represented in numbers are α-latrotoxins, 𝛿-latroinsectotoxins and latrodectins, which were first characterised from black widow venoms. Approximately two-thirds of the venom is composed of Latrodectus-like toxins. We present symptomology from 23 cases (15 unpublished) of S.nobilis envenomations confirming necrosis and Latrodectus-like symptoms such as debilitating pain, tremors, fatigue, nausea and hypotension. The continued rising numbers of S. nobilis will undoubtedly result in further bites and this study will help provide the medical community with a better understanding of the potential medical outcomes from bites by this species and alert them to the possibility of medically important outcomes. [less ▲]

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See detailEffect of ion counts stability during dynamically harmonized FT-ICR-MSI
Tiquet, Mathieu ULiege; La Rocca, Raphaël ULiege; Far, Johann ULiege et al

Poster (2019, April 01)

Mass spectrometry imaging of complex biological samples often require high spectral resolution and mass accuracy to properly distinguish all isobaric compounds. To achieve such requirement dynamically ... [more ▼]

Mass spectrometry imaging of complex biological samples often require high spectral resolution and mass accuracy to properly distinguish all isobaric compounds. To achieve such requirement dynamically harmonized FT-ICR analysers offer best results. However, mass accuracy below expectation due to masses shifting between pixels observed when performing image acquisitions. In this work we show a link between the mass shifting phenomenon andd the large variations observed in total ion current during image acquisitions. This work propose solve the mass shift by optimisation in sample preparation and acquisition parameters to stabilise the fluctuation of the total ion current in FT-ICR-MSI. [less ▲]

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See detailProteome of fraction from Tityus serrulatus venom reveals new enzymes and toxins
Amorim, F. G.; Longhim, H. T.; Cologna, C. T. et al

in Journal of Venomous Animals and Toxins Including Tropical Diseases (2019), 25

Background: Tityus serrulatus venom (Ts venom) is a complex mixture of several compounds with biotechnological and therapeutical potentials, which highlights the importance of the identification and ... [more ▼]

Background: Tityus serrulatus venom (Ts venom) is a complex mixture of several compounds with biotechnological and therapeutical potentials, which highlights the importance of the identification and characterization of these components. Although a considerable number of studies have been dedicated to the characterization of this complex cocktail, there is still a limitation of knowledge concerning its venom composition. Most of Ts venom studies aim to isolate and characterize their neurotoxins, which are small, basic proteins and are eluted with high buffer concentrations on cation exchange chromatography. The first and largest fraction from carboxymethyl cellulose-52 (CMC-52) chromatography of Ts venom, named fraction I (Fr I), is a mixture of proteins of high and low molecular masses, which do not interact with the cation exchange resin, being therefore a probable source of components still unknown of this venom. Thus, the present study aimed to perform the proteome study of Fraction I from Ts venom, by high resolution mass spectrometry, and its biochemical characterization, by the determination of several enzymatic activities. Methods: Fraction I was obtained by a cation exchange chromatography using 50 mg of crude venom. This fraction was subjected to a biochemical characterization, including determination of L-amino acid oxidase, phospholipase, hyaluronidase, proteases activities and inhibition of angiotensin converting enzyme (ACE) activity. Fraction I was submitted to reduction, alkylation and digestion processes, and the tryptic digested peptides obtained were analyzed in a Q-Exactive Orbitrap mass spectrometer. Data analysis was performed by PEAKS 8.5 software against NCBI database. Results: Fraction I exhibits proteolytic activity and it was able to inhibit ACE activity. Its proteome analysis identified 8 different classes of venom components, among them: neurotoxins (48%), metalloproteinases (21%), hypotensive peptides (11%), cysteine-rich venom protein (9%), antimicrobial peptides (AMP), phospholipases and other enzymes (chymotrypsin and lysozymes) (3%) and phosphodiesterases (2%). Conclusions: The combination of a proteomic and biochemical characterization strategies leads us to identify new components in the T. serrulatus scorpion venom. The proteome of venom's fraction can provide valuable direction in the obtainment of components in their native forms in order to perform a preliminary characterization and, consequently, to promote advances in biological discoveries in toxinology. © The Author(s). [less ▲]

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See detailAnalytical tool for lipopeptide identification
Mc Cann, Andréa ULiege; Kune, Christopher ULiege; Far, Johann ULiege et al

Conference (2018, November 30)

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See detailCombination of Capillary Electrophoresis and Ion mobility coupled to Mass Spectrometry and Theoretical Calculations for cysteine connectivity identification in peptides bearing two intra-molecular disulfide bonds
Delvaux, Cédric ULiege; Massonnet, Philippe ULiege; Kune, Christopher ULiege et al

Conference (2018, November 06)

Disulfide bonds are post translational modification playing essential roles in the biological activity and stability of numerous peptides and proteins. Intra-molecular disulfide bonds are found in various ... [more ▼]

Disulfide bonds are post translational modification playing essential roles in the biological activity and stability of numerous peptides and proteins. Intra-molecular disulfide bonds are found in various natural-occurring peptides such as animal venoms. In such peptides, the appropriate cysteine connectivity provides the required conformation for efficient binding to their molecular targets, which ensures their bioactivity. The characterization of cysteine pairing is still a challenging issue in the analysis of peptides targeting pharmaceutical or pharmacological utilizations. Thus, the use of sensitive, robust and efficient characterization techniques to access the cysteine pairing is crucial. In our workflow,the separation of the disulfide isomers of three peptides bearing two intra-molecular disulfide bonds but different cysteine connectivities have been tested using Capillary Zone Electrophoresis (CZE) and Ion Mobility (IM) coupled to Mass Spectrometry (MS). Results show that CZE-MS and IM-MS act as complementary techniques to unambiguously determine the cysteine connectivity of a given peptide. Indeed, the combination of the relative migration time to a reference peptide in CZE-MS, the drift time in IM-MS and the generation of fragments by Collision Induced Dissociation (CID) led to the attribution of the disulfide connectivities in all studied cases. Finally, theoretical calculations were performed to model the different structures in gas phase and solution, supporting the experimental observations on the basis of the predicted physicochemical properties. [less ▲]

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See detailExploitation de la plateforme e-Campus pour l’apprentissage de la Chimie de Première année pour les étudiants non acquis à la matière
Kune, Christopher ULiege; Quinton, Loïc ULiege

Scientific conference (2017, November 23)

De nos jours, les étudiants sont de plus en plus ouverts à l’e-Learning. La plateforme e-Campus, de par sa facilité à rendre disponible des contenus et des activés en ligne, permet à tout corps enseignant ... [more ▼]

De nos jours, les étudiants sont de plus en plus ouverts à l’e-Learning. La plateforme e-Campus, de par sa facilité à rendre disponible des contenus et des activés en ligne, permet à tout corps enseignant de répondre à cette demande grandissante. Pour les étudiants en première année de kinésithérapie et sciences de la motricité, l’e-Learning est devenu un complément incontournable du cours de Chimie. Lors de cette présentation, nous aborderons le développement de ce projet E-Learning pour le cours de chimie, de l’idée à la réalisation, en découvrant les outils offerts par la plateforme E-Campus, tels les questionnaires en ligne, les forums, les médiathèques… [less ▲]

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See detailThe usefulness of Ion Mobility-Mass Spectrometry for Small Molecules Analysis
Far, Johann ULiege; Goscinny, Séverine ULiege; Joly, Laure et al

Conference (2012, March)

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