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Aeonium is a genus of succulents belonging to the Crassulaceae family. Their importance in traditional medicine has stimulated both pharmacological and chemical research. In this study, we optimized extraction, separation, and analytical conditions using a high performance liquid chromatographic method coupled with electrospray ionization mass spectrometry by the negative mode (HPLC-ESI-MS) in order to, for the first time, determine thirty-four compounds from Aeonium arboreum leaves. Twenty-one of them are assigned among which are sixteen flavonoids and five phenolic acids. FRAP, TAC, DPPH, and ABTS•+ radical scavenging were used to evaluate antioxidant activity. The obtained IC50 values ranged from 0.031 to 0.043 mg.mL−1 for DPPH and between 0.048 and 0.09 mg·mL−1 for ABTS•+. Antimicrobial activity was also assessed. The obtained minimum inhibitory concentrations (MIC) of these extracts ranged from 12.5 to 50 µg·mL−1 against Micrococcus luteus, Listeria ivanovii, Staphylococcus aureus, Salmonella enterica, Escherichia coli, Pseudomonas aeruginosa, Aspergillus niger, and Fusarium oxysporum, and from 25 to 50 µg·mL−1 against Candida albicans. Therefore, these extracts can be considered as a potential source of biological active compounds.
Sahar Affes; Amer Ben Younes; Donyez Frikha; Noureddine Allouche; Michel Treilhou; Nathan Tene; Raoudha Mezghani-Jarraya. ESI-MS/MS Analysis of Phenolic Compounds from Aeonium arboreum Leaf Extracts and Evaluation of their Antioxidant and Antimicrobial Activities. Molecules 2021, 26, 4338 .
AMA StyleSahar Affes, Amer Ben Younes, Donyez Frikha, Noureddine Allouche, Michel Treilhou, Nathan Tene, Raoudha Mezghani-Jarraya. ESI-MS/MS Analysis of Phenolic Compounds from Aeonium arboreum Leaf Extracts and Evaluation of their Antioxidant and Antimicrobial Activities. Molecules. 2021; 26 (14):4338.
Chicago/Turabian StyleSahar Affes; Amer Ben Younes; Donyez Frikha; Noureddine Allouche; Michel Treilhou; Nathan Tene; Raoudha Mezghani-Jarraya. 2021. "ESI-MS/MS Analysis of Phenolic Compounds from Aeonium arboreum Leaf Extracts and Evaluation of their Antioxidant and Antimicrobial Activities." Molecules 26, no. 14: 4338.
Ants use venom for predation, defense, and communication; however, the molecular diversity, function, and potential applications of ant venom remains understudied compared to other venomous lineages such as arachnids, snakes and cone snails. In this work, we used a multidisciplinary approach that encompassed field work, proteomics, sequencing, chemical synthesis, structural analysis, molecular modeling, stability studies, and in vitro and in vivo bioassays to investigate the molecular diversity of the venom of the Amazonian Pseudomyrmex penetrator ants. We isolated a potent insecticidal heterodimeric peptide Δ-pseudomyrmecitoxin-Pp1a (Δ-PSDTX-Pp1a) composed of a 27-residue long A-chain and a 33-residue long B-chain cross-linked by two disulfide bonds in an antiparallel orientation. We chemically synthesized Δ-PSDTX-Pp1a, its corresponding parallel AA and BB homodimers, and its monomeric chains and demonstrated that Δ-PSDTX-Pp1a had the most potent insecticidal effects in blowfly assays (LD50 = 3 nmol/g). Molecular modeling and circular dichroism studies revealed strong α-helical features, indicating its cytotoxic effects could derive from cell membrane pore formation or disruption. The native heterodimer was substantially more stable against proteolytic degradation (t1/2 = 13 h) than its homodimers or monomers (t1/2 < 20 min), indicating an evolutionary advantage of the more complex structure. The proteomic analysis of Pseudomyrmex penetrator venom and in-depth characterization of Δ-PSDTX-Pp1a provide novel insights in the structural complexity of ant venom and further exemplifies how nature exploits disulfide-bond formation and dimerization to gain an evolutionary advantage via improved stability, a concept that is highly relevant for the design and development of peptide therapeutics, molecular probes, and bioinsecticides.
Axel Touchard; Helen C. Mendel; Isabelle Boulogne; Volker Herzig; Nayara Braga Emidio; Glenn F. King; Mathilde Triquigneaux; Lucie Jaquillard; Rémy Beroud; Michel De Waard; Olivier Delalande; Alain Dejean; Markus Muttenthaler; Christophe Duplais. Heterodimeric Insecticidal Peptide Provides New Insights into the Molecular and Functional Diversity of Ant Venoms. ACS Pharmacology & Translational Science 2020, 3, 1211 -1224.
AMA StyleAxel Touchard, Helen C. Mendel, Isabelle Boulogne, Volker Herzig, Nayara Braga Emidio, Glenn F. King, Mathilde Triquigneaux, Lucie Jaquillard, Rémy Beroud, Michel De Waard, Olivier Delalande, Alain Dejean, Markus Muttenthaler, Christophe Duplais. Heterodimeric Insecticidal Peptide Provides New Insights into the Molecular and Functional Diversity of Ant Venoms. ACS Pharmacology & Translational Science. 2020; 3 (6):1211-1224.
Chicago/Turabian StyleAxel Touchard; Helen C. Mendel; Isabelle Boulogne; Volker Herzig; Nayara Braga Emidio; Glenn F. King; Mathilde Triquigneaux; Lucie Jaquillard; Rémy Beroud; Michel De Waard; Olivier Delalande; Alain Dejean; Markus Muttenthaler; Christophe Duplais. 2020. "Heterodimeric Insecticidal Peptide Provides New Insights into the Molecular and Functional Diversity of Ant Venoms." ACS Pharmacology & Translational Science 3, no. 6: 1211-1224.
Ants use venom for predation, defence and communication, however, the molecular diversity, function and potential applications of ant venom remains understudied compared to other venomous lineages such as arachnids, snakes and cone snails. In this work, we used a multidisciplinary approach that encompassed field work, proteomics, sequencing, chemical synthesis, structural analysis, molecular modelling, stability studies, and a series ofin vitroandin vivobioassays to investigate the molecular diversity of the venom of the AmazonianPseudomyrmex penetratorants. We isolated a potent insecticidal heterodimeric peptide Δ-pseudomyrmecitoxin-Pp1a (Δ-PSDTX-Pp1a) composed of a 27-residue long A-chain and a 33-residue long B-chain crosslinked by two disulfide bonds in an antiparallel orientation. We chemically synthesised Δ-PSDTX-Pp1a, its corresponding parallel AA and BB homodimers, and its monomeric chains and demonstrated that Δ-PSDTX-Pp1a had the most potent insecticidal effects in blow fly assays (LD50= 3 nM). Molecular modelling and circular dichroism studies revealed strong alpha-helical features, indicating its cytotoxic effects could derive from membrane disruption, which was further supported by insect cell calcium assays. The native heterodimer was also substantially more stable against proteolytic degradation (t1/2=13 h) than its homodimers or monomers (t1/2<20 min), indicating an evolutionary advantage of the more complex structure. The proteomic analysis ofPseudomyrmex penetratorvenom and in-depth characterisation of Δ-PSDTX-Pp1a provide novel insights in the structural complexity of ant venom, and further exemplifies how nature exploits disulfide-bond formation and dimerization to gain an evolutionary advantageviaimproved stability; a concept that is also highly relevant for the design and development of peptide therapeutics, molecular probes and bioinsecticides.
Axel Touchard; Helen C. Mendel; Isabelle Boulogne; Volker Herzig; Nayara Braga Emidio; Glenn F. King; Mathilde Triquigneaux; Lucie Jaquillard; Rémy Béroud; Michel De Waard; Olivier Delalande; Alain Dejean; Markus Muttenthaler; Christophe Duplais. Heterodimeric insecticidal peptide provides new insights into the molecular and functional diversity of ant venoms. 2020, 1 .
AMA StyleAxel Touchard, Helen C. Mendel, Isabelle Boulogne, Volker Herzig, Nayara Braga Emidio, Glenn F. King, Mathilde Triquigneaux, Lucie Jaquillard, Rémy Béroud, Michel De Waard, Olivier Delalande, Alain Dejean, Markus Muttenthaler, Christophe Duplais. Heterodimeric insecticidal peptide provides new insights into the molecular and functional diversity of ant venoms. . 2020; ():1.
Chicago/Turabian StyleAxel Touchard; Helen C. Mendel; Isabelle Boulogne; Volker Herzig; Nayara Braga Emidio; Glenn F. King; Mathilde Triquigneaux; Lucie Jaquillard; Rémy Béroud; Michel De Waard; Olivier Delalande; Alain Dejean; Markus Muttenthaler; Christophe Duplais. 2020. "Heterodimeric insecticidal peptide provides new insights into the molecular and functional diversity of ant venoms." , no. : 1.
Ziram, a zinc dithiocarbamate is widely used worldwide as a fungicide in agriculture. In order to investigate ziram-induced changes in macrophage functions and polarization, human monocytes-derived macrophages in culture were treated with ziram at 0.01–10 μmol.L−1 for 4–24 h. To characterize zinc involvement in these changes, we also determined the effects of disulfiram alone (dithiocarbamate without zinc) or in co-incubation with ZnSO4. We have shown that ziram and disulfiram at 0.01 μmol.L−1 increased zymosan phagocytosis. In contrast, ziram at 10 μmol.L−1 completely inhibited this phagocytic process, the oxidative burst triggered by zymosan and the production of TNF-α, IL-1β, IL-6, and CCL2 triggered by LPS. Disulfiram had the same effects on these macrophages functions only when combined with zinc (10 μmol.L−1). In contrast, at 10 μmol.L−1 ziram and zinc associated-disulfiram induced expression of several antioxidants genes HMOX1, SOD2, and catalase, which could suggest the induction of oxidative stress. This oxidative stress could be involved in the increase in late apoptosis induced by ziram (10 μmol.L−1) and zinc associated-disulfiram. Concerning gene expression profiles of membrane markers of macrophage polarization, ziram at 10 μmol.L−1 had two opposite effects. It inhibited the gene expression of M2 markers (CD36, CD163) in the same way as the disulfiram-zinc co-treatment. Conversely, ziram induced gene expression of other M2 markers CD209, CD11b, and CD16 in the same way as treatment with zinc alone. Disulfiram-zinc association had no significant effects on these markers. These results taken together show that ziram via zinc modulates macrophages to M2-like anti-inflammatory phenotype which is often associated with various diseases.
Melissa Parny; José Bernad; Mélissa Prat; Marie Salon; Agnès Aubouy; Elsa Bonnafé; Agnès Coste; Bernard Pipy; Michel Treilhou. Comparative study of the effects of ziram and disulfiram on human monocyte-derived macrophage functions and polarization: involvement of zinc. Cell Biology and Toxicology 2020, 37, 379 -400.
AMA StyleMelissa Parny, José Bernad, Mélissa Prat, Marie Salon, Agnès Aubouy, Elsa Bonnafé, Agnès Coste, Bernard Pipy, Michel Treilhou. Comparative study of the effects of ziram and disulfiram on human monocyte-derived macrophage functions and polarization: involvement of zinc. Cell Biology and Toxicology. 2020; 37 (3):379-400.
Chicago/Turabian StyleMelissa Parny; José Bernad; Mélissa Prat; Marie Salon; Agnès Aubouy; Elsa Bonnafé; Agnès Coste; Bernard Pipy; Michel Treilhou. 2020. "Comparative study of the effects of ziram and disulfiram on human monocyte-derived macrophage functions and polarization: involvement of zinc." Cell Biology and Toxicology 37, no. 3: 379-400.
Phospholipase-A (PLA) enzymes catalyze the hydrolysis of ester bonds in select glycerophospholipids. Sensors for rapidly measuring the PLA activity in biological samples have relevance in the study of venom compositions and in medical diagnostics for the diagnosis of diseases such as acute pancreatitis. Current PLA sensor technologies are often restricted by the time it takes to prepare an assay, the necessity of using fluorescent labels, or the fact they might require strict pH control of the buffer vehicles used. Here we present a tethered bilayer lipid membrane (tBLM) impedance sensor array for the rapid and real-time detection of PLA, which includes the ability to selectively detect phospholipase-A2 (PLA2) from phospholipase-A1 (PLA1) isoforms. Comparing the activity of PLA1 and PLA2 in an array of tBLMs composed of ether phospholipids, ester phospholipids or ether-ester phospholipids allows for the rapid and reliable distinction between the isoforms, as measured using swept-frequency electrical impedance spectroscopy. After testing the assay using pure enzymes, we demonstrate the capacity of the sensor to identify specific PLA2-type, calcium-dependent activity from the venom of the South American bullet ant, Paraponera clavata, at a concentration of 1 μg/mL. The specificity of the phospholipase activity was corroborated using matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry. As further validation, we tested the activities of a PLA1 isoform in the presence of different buffers commonly used in biology and biochemistry experiments. Sensitivity testing shows that PLA1 can be detected at an activity as low as 0.06 U/mL. The rapid and reliable detection of phospholipases presented in this study has potential applications in the study of animal venoms as well as in lipase bioreactors and point-of-care devices.
Alvaro Garcia; Evelyne Deplazes; Samira R Aili; Matthew P. Padula; Axel Touchard; Christopher Murphy; Upeksha Mirissa Lankage; Graham M. Nicholson; Bruce Cornell; Charles G. Cranfield. Label-Free, Real-Time Phospholipase-A Isoform Assay. ACS Biomaterials Science & Engineering 2020, 6, 4714 -4721.
AMA StyleAlvaro Garcia, Evelyne Deplazes, Samira R Aili, Matthew P. Padula, Axel Touchard, Christopher Murphy, Upeksha Mirissa Lankage, Graham M. Nicholson, Bruce Cornell, Charles G. Cranfield. Label-Free, Real-Time Phospholipase-A Isoform Assay. ACS Biomaterials Science & Engineering. 2020; 6 (8):4714-4721.
Chicago/Turabian StyleAlvaro Garcia; Evelyne Deplazes; Samira R Aili; Matthew P. Padula; Axel Touchard; Christopher Murphy; Upeksha Mirissa Lankage; Graham M. Nicholson; Bruce Cornell; Charles G. Cranfield. 2020. "Label-Free, Real-Time Phospholipase-A Isoform Assay." ACS Biomaterials Science & Engineering 6, no. 8: 4714-4721.
A critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used to assign the tandem mass spectrometry (MS) fragmentation spectra of venom peptides and proteins to specific transcripts. This was performed alongside a shotgun liquid chromatography–mass spectrometry (LC-MS/MS) analysis of the venom to confirm that these assigned transcripts were expressed as proteins. Through the combined transcriptomic and proteomic investigation of Paraponera clavata venom, we identified four times the number of proteins previously identified using 2D-PAGE alone. In addition to this, by mining the transcriptomic data, we identified several novel peptide sequences for future pharmacological investigations, some of which conform with inhibitor cysteine knot motifs. These types of peptides have the potential to be developed into pharmaceutical or bioinsecticide peptides.
Samira R. Aili; Axel Touchard; Regan Hayward; Samuel D. Robinson; Sandy S. Pineda; Hadrien Lalagüe; Irina Vetter; Eivind A. B. Undheim; R. Manjunatha Kini; Pierre Escoubas; Matthew P. Padula; Garry S. A. Myers; Graham M. Nicholson. An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant Paraponera clavata. Toxins 2020, 12, 324 .
AMA StyleSamira R. Aili, Axel Touchard, Regan Hayward, Samuel D. Robinson, Sandy S. Pineda, Hadrien Lalagüe, Irina Vetter, Eivind A. B. Undheim, R. Manjunatha Kini, Pierre Escoubas, Matthew P. Padula, Garry S. A. Myers, Graham M. Nicholson. An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant Paraponera clavata. Toxins. 2020; 12 (5):324.
Chicago/Turabian StyleSamira R. Aili; Axel Touchard; Regan Hayward; Samuel D. Robinson; Sandy S. Pineda; Hadrien Lalagüe; Irina Vetter; Eivind A. B. Undheim; R. Manjunatha Kini; Pierre Escoubas; Matthew P. Padula; Garry S. A. Myers; Graham M. Nicholson. 2020. "An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant Paraponera clavata." Toxins 12, no. 5: 324.
Although ants are amongst the most abundant venomous terrestrial organisms, only a few studies have investigated the entire repertoire of peptides in the venom of a single ant species, or identified the toxins involved in insecticidal activity. In this study, the venom peptidome of the red ant, Manica rubida, was characterized using an integrated transcriptomic and proteomic approach. In addition, insecticidal assays of reversed-phase HPLC venom fractions were conducted on Lucilia caesar blowflies to identify toxic peptides. Thirteen myrmicitoxins were identified sharing sequence similarities to a number of other ant venom peptides. One myrmicitoxin was identified as an EGF-like toxin that is likely modified by O-fucosylation of a threonine residue. Six myrmicitoxins (i.e. U3-, U10-, U13-, U20-MYRTX-Mri1a, U10-MYRTX-Mri1b, and U10-MYRTX-Mri1c) present in HPLC fractions were responsible for the insecticidal activity. Chemically synthesized U10- MYRTX-Mri1a, -Mri1b, -Mri1c and U20-MYRTX-Mri1a irreversibly paralyzed blowflies at the highest doses tested (30 to 125 nmol.g-1) while, U13-MYRTX-Mri1a, the most potent neurotoxic peptide at 1 h, had reversible effects after 24 h (150 nmol.g-1). No insecticidal activity was noted for U3-MYRTX-Mri1a up to 55 nmol.g-1. We demonstrate that M. rubida employs a paralytic venom rich in linear insecticidal peptides which likely act by disrupting cell membranes.
Axel Touchard; Samira R. Aili; Nathan Téné; Valentine Barassé; Christophe Klopp; Alain Dejean; R. Manjunatha Kini; Mrinalini Mrinalini; Laurent Coquet; Thierry Jouenne; Benjamin Lefranc; Jérôme Leprince; Pierre Escoubas; Graham M. Nicholson; Michel Treilhou; Elsa Bonnafé. Venom Peptide Repertoire of the European Myrmicine Ant Manica rubida: Identification of Insecticidal Toxins. Journal of Proteome Research 2020, 19, 1800 -1811.
AMA StyleAxel Touchard, Samira R. Aili, Nathan Téné, Valentine Barassé, Christophe Klopp, Alain Dejean, R. Manjunatha Kini, Mrinalini Mrinalini, Laurent Coquet, Thierry Jouenne, Benjamin Lefranc, Jérôme Leprince, Pierre Escoubas, Graham M. Nicholson, Michel Treilhou, Elsa Bonnafé. Venom Peptide Repertoire of the European Myrmicine Ant Manica rubida: Identification of Insecticidal Toxins. Journal of Proteome Research. 2020; 19 (4):1800-1811.
Chicago/Turabian StyleAxel Touchard; Samira R. Aili; Nathan Téné; Valentine Barassé; Christophe Klopp; Alain Dejean; R. Manjunatha Kini; Mrinalini Mrinalini; Laurent Coquet; Thierry Jouenne; Benjamin Lefranc; Jérôme Leprince; Pierre Escoubas; Graham M. Nicholson; Michel Treilhou; Elsa Bonnafé. 2020. "Venom Peptide Repertoire of the European Myrmicine Ant Manica rubida: Identification of Insecticidal Toxins." Journal of Proteome Research 19, no. 4: 1800-1811.
In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and causing intense pain to browsing mammals. Using integrated transcriptomic and proteomic approaches, we identified the venom peptidome of the plant-ant Tetraponera aethiops (Pseudomyrmecinae). The transcriptomic analysis of its venom glands revealed that 40% of the expressed contigs encoded only seven peptide precursors related to the ant venom peptides from the A-superfamily. Among the 12 peptide masses detected by liquid chromatography-mass spectrometry (LC–MS), nine mature peptide sequences were characterized and confirmed through proteomic analysis. These venom peptides, called pseudomyrmecitoxins (PSDTX), share amino acid sequence identities with myrmeciitoxins known for their dual offensive and defensive functions on both insects and mammals. Furthermore, we demonstrated through reduction/alkylation of the crude venom that four PSDTXs were homo- and heterodimeric. Thus, we provide the first insights into the defensive venom composition of the ant genus Tetraponera indicative of a streamlined peptidome.
Valentine Barassé; Axel Touchard; Nathan Téné; Maurice Tindo; Martin Kenne; Christophe Klopp; Alain Dejean; Elsa Bonnafé; Michel Treilhou. The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae). Toxins 2019, 11, 732 .
AMA StyleValentine Barassé, Axel Touchard, Nathan Téné, Maurice Tindo, Martin Kenne, Christophe Klopp, Alain Dejean, Elsa Bonnafé, Michel Treilhou. The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae). Toxins. 2019; 11 (12):732.
Chicago/Turabian StyleValentine Barassé; Axel Touchard; Nathan Téné; Maurice Tindo; Martin Kenne; Christophe Klopp; Alain Dejean; Elsa Bonnafé; Michel Treilhou. 2019. "The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)." Toxins 11, no. 12: 732.
The peptide toxins in the venoms of small invertebrates such as stinging ants have rarely been studied due to the limited amount of venom available per individual. We used a venomics strategy to identify the molecular diversity of the venom peptidome for the myrmicine ant Tetramorium bicarinatum. The methodology included (i) peptidomics, in which the venom peptides are sequenced through a de novo mass spectrometry approach or Edman degradation; (ii) transcriptomics, based on RT-PCR-cloning and DNA sequencing; and (iii) the data mining of the RNA-seq in the available transcriptome. Mass spectrometry analysis revealed about 2800 peptides in the venom. However, the de novo sequencing suggested that most of these peptides arose from processing or the artifactual fragmentations of full-length mature peptides. These peptides, called “myrmicitoxins”, are produced by a limited number of genes. Thirty-seven peptide precursors were identified and classified into three superfamilies. These precursors are related to pilosulin, secapin or are new ant venom prepro-peptides. The mature myrmicitoxins display sequence homologies with antimicrobial, cytolytic and neurotoxic peptides. The venomics strategy enabled several post-translational modifications in some peptides such as O-glycosylation to be identified. This study provides novel insights into the molecular diversity and evolution of ant venoms.
Axel Touchard; Nathan Téné; Philippe Chan Tchi Song; Benjamin Lefranc; Jérôme Leprince; Michel Treilhou; Elsa Bonnafé. Deciphering the Molecular Diversity of an Ant Venom Peptidome through a Venomics Approach. Journal of Proteome Research 2018, 17, 3503 -3516.
AMA StyleAxel Touchard, Nathan Téné, Philippe Chan Tchi Song, Benjamin Lefranc, Jérôme Leprince, Michel Treilhou, Elsa Bonnafé. Deciphering the Molecular Diversity of an Ant Venom Peptidome through a Venomics Approach. Journal of Proteome Research. 2018; 17 (10):3503-3516.
Chicago/Turabian StyleAxel Touchard; Nathan Téné; Philippe Chan Tchi Song; Benjamin Lefranc; Jérôme Leprince; Michel Treilhou; Elsa Bonnafé. 2018. "Deciphering the Molecular Diversity of an Ant Venom Peptidome through a Venomics Approach." Journal of Proteome Research 17, no. 10: 3503-3516.
The venom peptide bicarinalin, previously isolated from the ant Tetramorium bicarinatum, is an antimicrobial agent with a broad spectrum of activity. In this study, we investigate the potential of bicarinalin as a novel agent against Helicobacter pylori, which causes several gastric diseases. First, the effects of synthetic bicarinalin have been tested against Helicobacter pylori: one ATCC strain, and forty-four isolated from stomach ulcer biopsies of Peruvian patients. Then the cytoxicity of bicarinalin on human gastric cells and murine peritoneal macrophages was measured using XTT and MTT assays, respectively. Finally, the preventive effect of bicarinalin was evaluated by scanning electron microscopy using an adherence assay of H. pylori on human gastric cells treated with bicarinalin. This peptide has a potent antibacterial activity at the same magnitude as four antibiotics currently used in therapies against H. pylori. Bicarinalin also inhibited adherence of H. pylori to gastric cells with an IC50 of 0.12 μg·mL−1 and had low toxicity for human cells. Scanning electron microscopy confirmed that bicarinalin can significantly decrease the density of H. pylori on gastric cells. We conclude that Bicarinalin is a promising compound for the development of a novel and effective anti-H. pylori agent for both curative and preventive use.
Jesus Guzman; Nathan Téné; Axel Touchard; Denis Castillo; Haouaria Belkhelfa; Laila Haddioui-Hbabi; Michel Treilhou; Michel Sauvain. Anti-Helicobacter pylori Properties of the Ant-Venom Peptide Bicarinalin. Toxins 2017, 10, 21 .
AMA StyleJesus Guzman, Nathan Téné, Axel Touchard, Denis Castillo, Haouaria Belkhelfa, Laila Haddioui-Hbabi, Michel Treilhou, Michel Sauvain. Anti-Helicobacter pylori Properties of the Ant-Venom Peptide Bicarinalin. Toxins. 2017; 10 (1):21.
Chicago/Turabian StyleJesus Guzman; Nathan Téné; Axel Touchard; Denis Castillo; Haouaria Belkhelfa; Laila Haddioui-Hbabi; Michel Treilhou; Michel Sauvain. 2017. "Anti-Helicobacter pylori Properties of the Ant-Venom Peptide Bicarinalin." Toxins 10, no. 1: 21.
Most ant venoms consist predominantly of small linear peptides, although some contain disulfide-linked peptides as minor components. However, in striking contrast to other ant species, some Anochetus venoms are composed primarily of disulfide-rich peptides. In this study, we investigated the venom of the ant Anochetus emarginatus with the aim of exploring these novel disulfide-rich peptides. The venom peptidome was initially investigated using a combination of reversed-phase HPLC and mass spectrometry, then the amino acid sequences of the major peptides were determined using a combination of Edman degradation and de novo MS/MS sequencing. We focused on one of these peptides, U1-PONTX-Ae1a (Ae1a), because of its novel sequence, which we predicted would form a novel 3D fold. Ae1a was chemically synthesized using Fmoc chemistry and its 3D structure was elucidated using NMR spectroscopy. The peptide was then tested for insecticidal activity and its effect on a range of human ion channels. Seven peptides named poneritoxins (PONTXs) were isolated and sequenced. The three-dimensional structure of synthetic Ae1a revealed a novel, compact scaffold in which a C-terminal β-hairpin is connected to the N-terminal region via two disulfide bonds. Synthetic Ae1a reversibly paralyzed blowflies and inhibited human L-type voltage-gated calcium channels (CaV1). Poneritoxins from Anochetus emarginatus venom are a novel class of toxins that are structurally unique among animal venoms. This study demonstrates that Anochetus ant venoms are a rich source of novel ion channel modulating peptides, some of which might be useful leads for the development of biopesticides.
Axel Touchard; Andreas Brust; Fernanda C Cardoso; Yanni Chin; Volker Herzig; Ai-Hua (Jean) Jin; Alain Dejean; Paul F. Alewood; Glenn King; Jérôme Orivel; Pierre Escoubas. Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus. Biochimica et Biophysica Acta (BBA) - General Subjects 2016, 1860, 2553 -2562.
AMA StyleAxel Touchard, Andreas Brust, Fernanda C Cardoso, Yanni Chin, Volker Herzig, Ai-Hua (Jean) Jin, Alain Dejean, Paul F. Alewood, Glenn King, Jérôme Orivel, Pierre Escoubas. Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus. Biochimica et Biophysica Acta (BBA) - General Subjects. 2016; 1860 (11):2553-2562.
Chicago/Turabian StyleAxel Touchard; Andreas Brust; Fernanda C Cardoso; Yanni Chin; Volker Herzig; Ai-Hua (Jean) Jin; Alain Dejean; Paul F. Alewood; Glenn King; Jérôme Orivel; Pierre Escoubas. 2016. "Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus." Biochimica et Biophysica Acta (BBA) - General Subjects 1860, no. 11: 2553-2562.
We have recently characterized bicarinalin as the most abundant peptide from the venom of the ant Tetramorium bicarinatum. This antimicrobial peptide is active against Staphylococcus and Enterobacteriaceae. To further investigate the antimicrobial properties of this cationic and cysteine-free peptide, we have studied its antibacterial, antifungal and antiparasitic activities on a large array of microorganisms. Bicarinalin was active against fifteen microorganisms with minimal inhibitory concentrations ranging from 2 and 25 μmol L−1. Cronobacter sakazakii, Salmonella enterica, Candida albicans, Aspergilus niger and Saccharomyces cerevisiae were particularly susceptible to this novel antimicrobial peptide. Resistant strains of Staphylococcus aureus, Pseudomonas aeruginosa and C. albicans were as susceptible as the canonical strains. Interestingly, bicarinalin was also active against the parasite Leishmania infantum with a minimal inhibitory concentrations of 2 μmol L−1. The bicarinalin pre-propeptide cDNA sequence has been determined using a combination of degenerated primers with RACE PCR strategy. Interestingly, the N-terminal domain of bicarinalin pre-propeptide exhibited sequence similarity with the pilosulin antimicrobial peptide family previously described in the Myrmecia venoms. Moreover, using SYTOX green uptake assay, we showed that, for all the tested microorganisms, bicarinalin acted through a membrane permeabilization mechanism. Two dimensional-NMR experiments showed that bicarinalin displayed a 10 residue-long α-helical structure flanked by two N- and C-terminal disordered regions. This partially amphipathic helix may explain the membrane permeabilization mechanism of bicarinalin observed in this study. Finally, therapeutic value of bicarinalin was highlighted by its low cytotoxicity against human lymphocytes at bactericidal concentrations and its long half-life in human serum which was around 15 h.
Nathan Téné; Elsa Bonnafé; Fanny Berger; Aline Rifflet; Laure Guilhaudis; Isabelle Ségalas-Milazzo; Bernard Pipy; Agnès Coste; Jérôme Leprince; Michel Treilhou. Biochemical and biophysical combined study of bicarinalin, an ant venom antimicrobial peptide. Peptides 2016, 79, 103 -113.
AMA StyleNathan Téné, Elsa Bonnafé, Fanny Berger, Aline Rifflet, Laure Guilhaudis, Isabelle Ségalas-Milazzo, Bernard Pipy, Agnès Coste, Jérôme Leprince, Michel Treilhou. Biochemical and biophysical combined study of bicarinalin, an ant venom antimicrobial peptide. Peptides. 2016; 79 ():103-113.
Chicago/Turabian StyleNathan Téné; Elsa Bonnafé; Fanny Berger; Aline Rifflet; Laure Guilhaudis; Isabelle Ségalas-Milazzo; Bernard Pipy; Agnès Coste; Jérôme Leprince; Michel Treilhou. 2016. "Biochemical and biophysical combined study of bicarinalin, an ant venom antimicrobial peptide." Peptides 79, no. : 103-113.
Ants (Formicidae) represent a taxonomically diverse group of hymenopterans with over 13,000 extant species, the majority of which inject or spray secretions from a venom gland. The evolutionary success of ants is mostly due to their unique eusociality that has permitted them to develop complex collaborative strategies, partly involving their venom secretions, to defend their nest against predators, microbial pathogens, ant competitors, and to hunt prey. Activities of ant venom include paralytic, cytolytic, haemolytic, allergenic, pro-inflammatory, insecticidal, antimicrobial, and pain-producing pharmacologic activities, while non-toxic functions include roles in chemical communication involving trail and sex pheromones, deterrents, and aggregators. While these diverse activities in ant venoms have until now been largely understudied due to the small venom yield from ants, modern analytical and venomic techniques are beginning to reveal the diversity of toxin structure and function. As such, ant venoms are distinct from other venomous animals, not only rich in linear, dimeric and disulfide-bonded peptides and bioactive proteins, but also other volatile and non-volatile compounds such as alkaloids and hydrocarbons. The present review details the unique structures and pharmacologies of known ant venom proteinaceous and alkaloidal toxins and their potential as a source of novel bioinsecticides and therapeutic agents.
Axel Touchard; Samira R. Aili; Eduardo Gonçalves Paterson Fox; Pierre Escoubas; Jérôme Orivel; Graham M. Nicholson; Alain Dejean. The Biochemical Toxin Arsenal from Ant Venoms. Toxins 2016, 8, 30 .
AMA StyleAxel Touchard, Samira R. Aili, Eduardo Gonçalves Paterson Fox, Pierre Escoubas, Jérôme Orivel, Graham M. Nicholson, Alain Dejean. The Biochemical Toxin Arsenal from Ant Venoms. Toxins. 2016; 8 (1):30.
Chicago/Turabian StyleAxel Touchard; Samira R. Aili; Eduardo Gonçalves Paterson Fox; Pierre Escoubas; Jérôme Orivel; Graham M. Nicholson; Alain Dejean. 2016. "The Biochemical Toxin Arsenal from Ant Venoms." Toxins 8, no. 1: 30.
In the Guianese rainforest, we examined the impact of the presence of guano in and around a bat roosting site (a cave). We used ant communities as an indicator to evaluate this impact because they occupy a central place in the functioning of tropical rainforest ecosystems and they play different roles in the food web as they can be herbivores, generalists, scavengers or predators. The ant species richness around the cave did not differ from a control sample situated 500m away. Yet, the comparison of functional groups resulted in significantly greater numbers of detritivorous fungus-growing and predatory ant colonies around the cave compared to the control, the contrary being true for nectar and honeydew feeders. The role of bats, through their guano, was shown using stable isotope analyses as we noted significantly greater δ(15)N values for the ant species captured in and around the cave compared to controls.
Alain Dejean; Sarah Groc; Bruno Herault; Héctor Rodríguez-Pérez; Axel Touchard; Régis Céréghino; Jacques H.C. Delabie; Bruno Corbara. Bat aggregation mediates the functional structure of ant assemblages. Comptes Rendus. Biologies 2015, 338, 688 -695.
AMA StyleAlain Dejean, Sarah Groc, Bruno Herault, Héctor Rodríguez-Pérez, Axel Touchard, Régis Céréghino, Jacques H.C. Delabie, Bruno Corbara. Bat aggregation mediates the functional structure of ant assemblages. Comptes Rendus. Biologies. 2015; 338 (10):688-695.
Chicago/Turabian StyleAlain Dejean; Sarah Groc; Bruno Herault; Héctor Rodríguez-Pérez; Axel Touchard; Régis Céréghino; Jacques H.C. Delabie; Bruno Corbara. 2015. "Bat aggregation mediates the functional structure of ant assemblages." Comptes Rendus. Biologies 338, no. 10: 688-695.
In this study, conducted in French Guiana, a part of the native range of the fire ant Solenopsis saevissima, we compared the cuticular hydrocarbon profiles of media workers with previous results based on intraspecific aggressiveness tests. We noted a strong congruence between the two studies permitting us to delimit two supercolonies extending over large distances (up to 54 km), a phenomenon known as unicoloniality. Solenopsis geminata workers, taken as an out‐group for cluster analyses, have a very different cuticular hydrocarbon profile. Because S. saevissima has been reported outside its native range, our conclusion is that this species has the potential to become invasive because unicoloniality (i.e., the main attribute for ants to become invasive) was shown at least for the Guianese population.
Alain Lenoir; Séverine Devers; Axel Touchard; Alain Dejean. The Guianese population of the fire ant Solenopsis saevissima is unicolonial. Insect Science 2015, 23, 739 -745.
AMA StyleAlain Lenoir, Séverine Devers, Axel Touchard, Alain Dejean. The Guianese population of the fire ant Solenopsis saevissima is unicolonial. Insect Science. 2015; 23 (5):739-745.
Chicago/Turabian StyleAlain Lenoir; Séverine Devers; Axel Touchard; Alain Dejean. 2015. "The Guianese population of the fire ant Solenopsis saevissima is unicolonial." Insect Science 23, no. 5: 739-745.
Michel Treilhou; Jean-François Chollet; Michel Couderchet. Crop protection, environment, health, and biodiversity: observations and outlook. Environmental Science and Pollution Research 2015, 22, 7987 -7990.
AMA StyleMichel Treilhou, Jean-François Chollet, Michel Couderchet. Crop protection, environment, health, and biodiversity: observations and outlook. Environmental Science and Pollution Research. 2015; 22 (11):7987-7990.
Chicago/Turabian StyleMichel Treilhou; Jean-François Chollet; Michel Couderchet. 2015. "Crop protection, environment, health, and biodiversity: observations and outlook." Environmental Science and Pollution Research 22, no. 11: 7987-7990.
Compared with other animal venoms, ant venoms remain little explored. Ants have evolved complex venoms to rapidly immobilize arthropod prey and to protect their colonies from predators and pathogens. Many ants have retained peptide‐rich venoms that are similar to those of other arthropod groups. With the goal of conducting a broad and comprehensive survey of ant venom peptide diversity, we investigated the peptide composition of venoms from 82 stinging ant species from nine subfamilies using matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry (MALDI‐TOFMS). We also conducted an in‐depth investigation of eight venoms using reversed‐phase high‐performance liquid chromatography (RP‐HPLC) separation coupled with offline MALDI‐TOFMS. Our results reveal that the peptide compositions of ant venom peptidomes from both poneroid and formicoid ant clades comprise hundreds of small peptides (4 kDa) are also present in the venom of formicoids. Chemical reduction revealed the presence of disulfide‐linked peptides in most ant subfamilies, including peptides structured by one, two or three disulfide bonds as well as dimeric peptides reticulated by three disulfide bonds. The biochemical complexity of ant venoms, associated with an enormous ecological and taxonomic diversity, suggests that stinging ant venoms constitute a promising source of bioactive molecules that could be exploited in the search for novel drug and biopesticide leads. Copyright © 2015 John Wiley & Sons, Ltd.
Axel Touchard; Jennifer M. S. Koh; Samira R. Aili; Alain Dejean; Graham Nicholson; Jerome Orivel; Pierre Escoubas. The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling. Rapid Communications in Mass Spectrometry 2015, 29, 385 -396.
AMA StyleAxel Touchard, Jennifer M. S. Koh, Samira R. Aili, Alain Dejean, Graham Nicholson, Jerome Orivel, Pierre Escoubas. The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling. Rapid Communications in Mass Spectrometry. 2015; 29 (5):385-396.
Chicago/Turabian StyleAxel Touchard; Jennifer M. S. Koh; Samira R. Aili; Alain Dejean; Graham Nicholson; Jerome Orivel; Pierre Escoubas. 2015. "The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling." Rapid Communications in Mass Spectrometry 29, no. 5: 385-396.
The rise of integrative taxonomy, a multi-criteria approach used in characterizing species, fosters the development of new tools facilitating species delimitation. Mass spectrometric (MS) analysis of venom peptides from venomous animals has previously been demonstrated to be a valid method for identifying species. Here we aimed to develop a rapid chemotaxonomic tool for identifying ants based on venom peptide mass fingerprinting. The study focused on the biodiversity of ponerine ants (Hymenoptera: Formicidae: Ponerinae) in French Guiana. Initial experiments optimized the use of automated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to determine variations in the mass profiles of ant venoms using several MALDI matrices and additives. Data were then analyzed via a hierarchical cluster analysis to classify the venoms of 17 ant species. In addition, phylogenetic relationships were assessed and were highly correlated with methods using DNA sequencing of the mitochondrial gene cytochrome c oxidase subunit 1. By combining a molecular genetics approach with this chemotaxonomic approach, we were able to improve the accuracy of the taxonomic findings to reveal cryptic ant species within species complexes. This chemotaxonomic tool can therefore contribute to more rapid species identification and more accurate taxonomies. This is the first extensive study concerning the peptide analysis of the venom of both Pachycondyla and Odontomachus ants. We studied the venoms of 17 ant species from French Guiana that permitted us to fine-tune the venom analysis of ponerine ants via MALDI-TOF mass spectrometry. We explored the peptidomes of crude ant venom and demonstrated that venom peptides can be used in the identification of ant species. In addition, the application of this novel chemotaxonomic method combined with a parallel genetic approach using COI sequencing permitted us to reveal the presence of cryptic ants within both the Pachycondyla apicalis and Pachycondyla stigma species complexes. This adds a new dimension to the search for means of exploiting the enormous biodiversity of venomous ants as a source for novel therapeutic drugs or biopesticides. This article is part of a Special Issue entitled: Proteomics of non-model organisms.
Axel Touchard; Mélodie Dauvois; Marie-Jeanne Arguel; Frédéric Petitclerc; Mathieu Leblanc; Alain Dejean; Jerome Orivel; Graham Nicholson; Pierre Escoubas. Elucidation of the unexplored biodiversity of ant venom peptidomes via MALDI–TOF mass spectrometry and its application for chemotaxonomy. Journal of Proteomics 2014, 105, 217 -231.
AMA StyleAxel Touchard, Mélodie Dauvois, Marie-Jeanne Arguel, Frédéric Petitclerc, Mathieu Leblanc, Alain Dejean, Jerome Orivel, Graham Nicholson, Pierre Escoubas. Elucidation of the unexplored biodiversity of ant venom peptidomes via MALDI–TOF mass spectrometry and its application for chemotaxonomy. Journal of Proteomics. 2014; 105 ():217-231.
Chicago/Turabian StyleAxel Touchard; Mélodie Dauvois; Marie-Jeanne Arguel; Frédéric Petitclerc; Mathieu Leblanc; Alain Dejean; Jerome Orivel; Graham Nicholson; Pierre Escoubas. 2014. "Elucidation of the unexplored biodiversity of ant venom peptidomes via MALDI–TOF mass spectrometry and its application for chemotaxonomy." Journal of Proteomics 105, no. : 217-231.
Thymol is a natural substance increasingly used as an alternative to pesticides in the fight against the Varroa destructor mite. Despite the effectiveness of this phenolic monoterpene against Varroa, few articles have covered the negative or side effects of thymol on bees. In a previous study, we have found an impairment of phototaxis in honeybees following application of sublethal doses of thymol—lower or equal to 100 ng/bee—under laboratory conditions. The present work shows the same behavioral effects on bees from hives treated with Apilife Var®, a veterinary drug containing 74 % thymol, with a decrease in phototactic behavior observed 1 day after treatment. Thus, thymol causes disruption of bee phototactic behavior both under laboratory conditions as well as in beehives. The bee exposure dose in treated hives was quantified using gas chromatography coupled to mass spectrometry (GC–MS), giving a median value of 4.3 μg per body 24 h after treatment, with 11 ng in the brain. The thymol level in 20 organic waxes from hives treated with Apilife Var® was also measured and showed that it persists in waxes (around 10 mg/kg) 1 year after treatment. Thus, in the light of (1) behavioral data obtained under laboratory conditions and in beehives, (2) the persistence of thymol in waxes, and (3) the high load on bees, it would appear important to study the long-term effects of thymol in beehives.
Jean-Luc Carayon; Nathan Téné; Elsa Bonnafé; Julie Alayrangues; Lucie Hotier; Catherine Armengaud; Michel Treilhou. Thymol as an alternative to pesticides: persistence and effects of Apilife Var on the phototactic behavior of the honeybee Apis mellifera. Environmental Science and Pollution Research 2013, 21, 4934 -4939.
AMA StyleJean-Luc Carayon, Nathan Téné, Elsa Bonnafé, Julie Alayrangues, Lucie Hotier, Catherine Armengaud, Michel Treilhou. Thymol as an alternative to pesticides: persistence and effects of Apilife Var on the phototactic behavior of the honeybee Apis mellifera. Environmental Science and Pollution Research. 2013; 21 (7):4934-4939.
Chicago/Turabian StyleJean-Luc Carayon; Nathan Téné; Elsa Bonnafé; Julie Alayrangues; Lucie Hotier; Catherine Armengaud; Michel Treilhou. 2013. "Thymol as an alternative to pesticides: persistence and effects of Apilife Var on the phototactic behavior of the honeybee Apis mellifera." Environmental Science and Pollution Research 21, no. 7: 4934-4939.
A novel antimicrobial peptide, named Bicarinalin, has been isolated from the venom of the ant Tetramorium bicarinatum. Its amino acid sequence has been determined by de novo sequencing using mass spectrometry and by Edman degradation. Bicarinalin contained 20 amino acid residues and was C-terminally amidated as the majority of antimicrobial peptides isolated to date from insect venoms. Interestingly, this peptide had a linear structure and exhibited no meaningful similarity with any known peptides. Antibacterial activities against Staphylococcus aureus and S. xylosus strains were evaluated using a synthetic replicate. Bicarinalin had a potent and broad antibacterial activity of the same magnitude as Melittin and other hymenopteran antimicrobial peptides such as Pilosulin or Defensin. Moreover, this antimicrobial peptide has a weak hemolytic activity compared to Melittin on erythrocytes, suggesting potential for development into an anti-infective agent for use against emerging antibiotic-resistant pathogens.
Aline Rifflet; Sabine Gavalda; Nathan Téné; Jérôme Orivel; Jérôme Leprince; Laure Guilhaudis; Eric Génin; Angélique Vétillard; Michel Treilhou. Identification and characterization of a novel antimicrobial peptide from the venom of the ant Tetramorium bicarinatum. Peptides 2012, 38, 363 -370.
AMA StyleAline Rifflet, Sabine Gavalda, Nathan Téné, Jérôme Orivel, Jérôme Leprince, Laure Guilhaudis, Eric Génin, Angélique Vétillard, Michel Treilhou. Identification and characterization of a novel antimicrobial peptide from the venom of the ant Tetramorium bicarinatum. Peptides. 2012; 38 (2):363-370.
Chicago/Turabian StyleAline Rifflet; Sabine Gavalda; Nathan Téné; Jérôme Orivel; Jérôme Leprince; Laure Guilhaudis; Eric Génin; Angélique Vétillard; Michel Treilhou. 2012. "Identification and characterization of a novel antimicrobial peptide from the venom of the ant Tetramorium bicarinatum." Peptides 38, no. 2: 363-370.