Pierre Escoubas

Université Côte d'Azur

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Graham M. Nicholson

University of Technology Sydney

Terumi Nakajima

Suntory Foundation for Life Sciences

Junya Mizutani

Hokkaido University

Labunmi Lajide

Federal University of Technology

Michel Lazdunski

Institut de Pharmacologie Moléculaire et Cellulaire

Gerardo Corzo

Universidad Nacional Autónoma de México

Glenn F. King

University of Queensland

Axel Touchard

Ecologie des Forêts de Guyane

Sylvie Diochot

Laboratoire d'Excellence Canaux Ioniques d'Intérêt Thérapeutique

Alain Déjean

Museo Nacional de Ciencias Naturales

Cooperative Institutions

Centre National de la Recherche Scientifique

102

University of Queensland

Institut de Pharmacologie Moléculaire et Cellulaire

Inserm

Université Côte d'Azur

Universiti Brunei Darussalam

Suntory Foundation for Life Sciences

University of Technology Sydney

University of Sydney

Monash University

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Venomics: unravelling the complexity of animal venoms with mass spectrometry

Journal of Mass Spectrometry (2008)

Pierre Escoubas Loïc Quinton Graham M. Nicholson

Abstract Animal venoms and toxins are now recognized as major sources of bioactive molecules that may be tomorrow's new drug leads. Their complexity and their potential as drug sources have been demonstrated by application of modern analytical technologies, which have revealed venoms to be vast peptide combinatorial libraries. Structural as well as pharmacological diversity is immense, and mass spectrometry is now one of the major investigative tools for the structural investigation of venom components. Recent advances in its use in the study of venom and toxins are reviewed. The application of mass spectrometry techniques to peptide toxin sequence determination by de novo sequencing is discussed in detail, in the light of the search for novel analgesic drugs. We also present the combined application of LC‐MALDI separation with mass fingerprinting and ISD fragmentation for the determination of structural and pharmacological classes of peptides in complex spider venoms. This approach now serves as the basis for the full investigation of complex spider venom proteomes, in combination with cDNA analysis. Copyright © 2008 John Wiley & Sons, Ltd.

Spider toxin

Proteome

10.1002/jms.1389

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Citations (152)

ChemInform Abstract: Termite Antifeedant Activity in Tropical Plants. Part 2. Termite Antifeedant Activity in Aframomum melegueta.

ChemInform (1996)

Pierre Escoubas Labunmi Lajide Junya Mizutani

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

10.1002/chin.199609310

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A Spider Toxin That Induces a Typical Effect of Scorpion α-Toxins but Competes with β-Toxins on Binding to Insect Sodium Channels

Biochemistry (2005)

Gerardo Corzo Pierre Escoubas Elba Villegas Izhar Karbat Dalia Gordon

δ-Palutoxins from the spider Paracoelotes luctuosus (Araneae: Amaurobiidae) are 36−37 residue long peptides that show preference for insect sodium channels (NaChs) and modulate their function. Although they slow NaCh inactivation in a fashion similar to that of receptor site 3 modifiers, such as scorpion α-toxins, they actually bind with high affinity to the topologically distinct receptor site 4 of scorpion β-toxins. To resolve this riddle, we scanned by Ala mutagenesis the surface of δ-PaluIT2, a δ-palutoxin variant with the highest affinity for insect NaChs, and compared it to the bioactive surface of a scorpion β-toxin. We found three regions on the surface of δ-PaluIT2 important for activity: the first consists of Tyr-22 and Tyr-30 (aromatic), Ser-24 and Met-28 (polar), and Arg-8, Arg-26, Arg-32, and Arg-34 (basic) residues; the second is made of Trp-12; and the third is made of Asp-19, whose substitution by Ala uncoupled the binding from toxicity to lepidopteran larvae. Although spider δ-palutoxins and scorpion β-toxins have developed from different ancestors, they show some commonality in their bioactive surfaces, which may explain their ability to compete for an identical receptor (site 4) on voltage-gated NaChs. Yet, their different mode of channel modulation provides a novel perspective about the structural relatedness of receptor sites 3 and 4, which until now have been considered topologically distinct.

Spider toxin

Scorpion toxin

Scorpion Venoms

10.1021/bi048434k

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Citations (38)

A comparison of matrix-assisted laser desorption/ionization time-of-flight and liquid chromatography electrospray ionization mass spectrometry methods for the analysis of crude tarantula venoms in thePterinochilus group

Rapid Communications in Mass Spectrometry (1999)

Pierre Escoubas Julia Chamot‐Rooke Reto Stöcklin Brian Whiteley Gerardo Corzo

The search for novel pharmacological tools in spider venoms involves the need for precise and reproducible species identification methods. As an addition to morphological analysis, we have developed venom fingerprinting by reversed-phase chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) as an efficient and precise venom identification tool. In order to compare the possible use of liquid chromatography electrospray ionization mass spectrometry (LC/ESI-MS) as an additional venom characterization tool, we have applied both methodologies to the study of several tarantula venom samples in the Pterinochilus murinus group. These species possess highly active venoms yet their taxonomy remains difficult. We demonstrate that both methodologies can be successfully applied to tarantula venom characterization. MALDI-TOFMS and ESI-MS gave similar overall profiles and allowed fine discrimination of samples. At least one venom sample was proven to belong to a completely different venom group. Coupling of ESI-MS with HPLC separation afforded a new dimension in venom analysis, with clear discrimination between components of similar Mr and gave a finer picture of venom composition, number of molecular species and molecular weight distribution. Copyright © 1999 John Wiley & Sons, Ltd.

Matrix (chemical analysis)

10.1002/(sici)1097-0231(19990930)13:18<1861::aid-rcm730>3.0.co;2-7

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Citations (44)

Unraveling the unexplored biochemical complexity of ant venoms

Axel Touchard Alain Déjean Jennifer Koh Graham M. Nicholson Pierre Escoubas

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Antifeedant activity of metabolites of Aristolochia albida against the tobacco cutworm, Spodoptera litura

Journal of Agricultural and Food Chemistry (1993)

Labunmi Lajide Pierre Escoubas Junya Mizutani

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAntifeedant activity of metabolites of Aristolochia albida against the tobacco cutworm, Spodoptera lituraLabunmi. Lajide, Pierre. Escoubas, and Junya. MizutaniCite this: J. Agric. Food Chem. 1993, 41, 4, 669–673Publication Date (Print):April 1, 1993Publication History Published online1 May 2002Published inissue 1 April 1993https://pubs.acs.org/doi/10.1021/jf00028a031https://doi.org/10.1021/jf00028a031research-articleACS PublicationsRequest reuse permissionsArticle Views237Altmetric-Citations34LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

Spodoptera litura

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10.1021/jf00028a031

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Citations (41)

Spider venom peptides as leads for drug and insecticide design

Editora UFMG eBooks (2009)

Frank Bosmans Pierre Escoubas Graham M. Nicholson

Spider toxin

Source

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Citations (6)

47. VENOMICS: High-throughput peptidomics and transcriptomics of animal venoms for discovery of novel therapeutic peptides

Toxicon (2014)

Marion Verdenaud Michel Degueldre S. Zúñiga Juan Carlos Triviño Loïc Quinton

10.1016/j.toxicon.2014.08.055

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Two novel short insectotoxins from the Asian scorpions Buthus martensi and Buthus tamulus

Toxicon (1997)

Pierre Escoubas R. Romi-Lebrun Fan Wu R. Herrmann H. Moskowitz

10.1016/s0041-0101(97)84748-4

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Citations (2)

Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton‐gated channels

Protein Science (2005)

Benjamin Chagot Pierre Escoubas Sylvie Diochot Cédric Bernard Michel Lazdunski

Acid-sensing ion channels (ASIC) are proton-gated sodium channels that have been implicated in pain transduction associated with acidosis in inflamed or ischemic tissues. APETx2, a peptide toxin effector of ASIC3, has been purified from an extract of the sea anemone Anthopleura elegantissima. APETx2 is a 42-amino-acid peptide cross-linked by three disulfide bridges. Its three-dimensional structure, as determined by conventional two-dimensional 1H-NMR, consists of a compact disulfide-bonded core composed of a four-stranded beta-sheet. It belongs to the disulfide-rich all-beta structural family encompassing peptide toxins commonly found in animal venoms. The structural characteristics of APETx2 are compared with that of PcTx1, another effector of ASIC channels but specific to the ASIC1a subtype and to APETx1, a toxin structurally related to APETx2, which targets the HERG potassium channel. Structural comparisons, coupled with the analysis of the electrostatic characteristics of these various ion channel effectors, led us to suggest a putative channel interaction surface for APETx2, encompassing its N terminus together with the type I-beta turn connecting beta-strands III and IV. This basic surface (R31 and R17) is also rich in aromatic residues (Y16, F15, Y32, and F33). An additional region made of the type II'-beta turn connecting beta-strands I and II could also play a role in the specificity observed for these different ion effectors.

Acid-sensing ion channel

Turn (biochemistry)

Ankyrin repeat

10.1110/ps.051378905

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Citations (63)