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H. Zerrouk

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Hervé Rochat

Bioénergétique et Ingénierie des Protéines

Marie‐France Martin‐Eauclaire

Centre de Recherche en Neurobiologie - Neurophysiologie de Marseille

Pascal Mansuelle

Centre National de la Recherche Scientifique

A. Benslimane

Sidi Mohamed Ben Abdellah University

J. Van Rietschoten

Centre National de la Recherche Scientifique

G Jacquet

Centre National de la Recherche Scientifique

Marcel Crest

Laboratoire de Neurosciences Cognitives

H. Darbon

Centre National de la Recherche Scientifique

Maurice Gola

Centre National de la Recherche Scientifique

Kamel Mabrouk

Institut de Chimie Radicalaire

Cooperative Institutions

Centre National de la Recherche Scientifique

Bioénergétique et Ingénierie des Protéines

Aix-Marseille Université

Inserm

Laboratoire de Biochimie

Roche (Switzerland)

Centre de Recherche en Neurobiologie - Neurophysiologie de Marseille

Roche (France)

Hôpital Nord

Institut de Neurobiologie de la Méditerranée

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Synthesis and characterization of kaliotoxin. Is the 26-32 sequence essential for potassium channel recognition?

Journal of Biological Chemistry (1993)

R. Romi Marcel Crest Maurice Gola F. Sampiéri G Jacquet

Kaliotoxin (KTX), a scorpion toxin characterized as a 37-residue inhibitor of the neuronal high conductance Ca(2+)-activated K+ channels (KCa channels), has been chemically synthetized. Differences were observed between natural toxin and the two peptides, KTX(1-37) and KTX(1-37)-amide. Re-examination of the KTX sequence showed that an extra lysine residue was present at the C-terminal end. The 38-residue synthetic peptide was found identical with natural toxin. All three peptides had comparable activities, with LD50 values of 6-9 pmol/mouse after intracerebroventricular injection, and Kd = 2-8 nM for blockage of the whole cell and unitary molluscan KCa currents. Pairing of the disulfide bonds in synthetic KTX corresponded to that in charybdotoxin and iberiotoxin. A competition assay between 125I-KTX(1-37) and different toxins (KTX, dendrotoxin, charybdotoxin, MCD peptide, and iberiotoxin) for binding to rat brain synaptosomal membranes suggested that KTX interacts also with voltage-gated K+ channels. Shorter peptides, KTX(25-35)-amide and KTX(26-32)-amide, expressed no KTX activity, but were able to compete in binding. They were further shown to antagonize KTX in both its toxicity and blocking activity. The (26-32) sequence of KTX, which is a highly conserved region, may contain a low affinity binding subsite essential for potassium channel recognition.

Sequence (biology)

Characterization

10.1016/s0021-9258(19)74315-4

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Citations (76)

P05, a new leiurotoxin I-like scorpion toxin: Synthesis and structure-activity relationships of the .alpha.-amidated analog, a ligand of calcium-activated potassium channels with increased affinity

Biochemistry (1993)

Jean‐Marc Sabatier H. Zerrouk H. Darbon Kamel Mabrouk A. Benslimane

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTP05, a new leiurotoxin I-like scorpion toxin: Synthesis and structure-activity relationships of the .alpha.-amidated analog, a ligand of calcium-activated potassium channels with increased affinityJ. M. Sabatier, H. Zerrouk, H. Darbon, K. Mabrouk, A. Benslimane, H. Rochat, M. F. Martin-Eauclaire, and J. Van RietschotenCite this: Biochemistry 1993, 32, 11, 2763–2770Publication Date (Print):March 23, 1993Publication History Published online1 May 2002Published inissue 23 March 1993https://pubs.acs.org/doi/10.1021/bi00062a005https://doi.org/10.1021/bi00062a005research-articleACS PublicationsRequest reuse permissionsArticle Views75Altmetric-Citations78LEARN 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

Alpha (finance)

Scorpion toxin

10.1021/bi00062a005

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Citations (96)

Growth inhibition of Trypanosoma cruzi and Leishmania donovani infantum by different snake venoms: Preliminary identification of proteins from Cerastes cerastes venom which interact with the parasites

Rodolfo Fernández H. Zerrouk Fatima Sebti Marc Loyens A. Benslimane

Viper Venoms

10.1016/0041-0101(94)90366-2

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Citations (44)

Study on P05, a new Leiurotoxin I scorpion toxin

Peptides (1994)

Jean‐Marc Sabatier H. Zerrouk H. Darbon Kamel Mabrouk A. Benslimane

Scorpion toxin

10.1007/978-94-011-0683-2_172

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Citations (0)

Characterization of a new leiurotoxin I‐like scorpion toxin

FEBS Letters (1993)

H. Zerrouk Pascal Mansuelle A. Benslimane Hervé Rochat Marie‐France Martin‐Eauclaire

Three novel peptide inhibitors of the SKCa channels were purified to homogeneity from the venom of the scorpion Androctonus mauretanicus mauretanicus using one step of RP-HPLC and competition assays with [125I]apamin to rat brain synaptosomes. PO1, PO2 and PO5 have K0.5 of 100, 100 and 0.02 nM, respectively, for the apamin binding site. The sequence of PO5 was established and compared to that of other scorpion toxins active on K+ channels: it contains 31 residues and has a free carboxyl end. it shares sequence similarity with apamin and leiurotoxin I.

Apamin

Scorpion toxin

Scorpion Venoms

10.1016/0014-5793(93)80583-g

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Citations (71)

Kaliotoxin, a novel peptidyl inhibitor of neuronal BK-type Ca(2+)-activated K+ channels characterized from Androctonus mauretanicus mauretanicus venom.

Journal of Biological Chemistry (1992)

Marcel Crest G Jacquet Maurice Gola H. Zerrouk A. Benslimane

A peptidyl inhibitor of the high conductance Ca(2+)-activated K+ channels (KCa) has been purified to homogeneity from the venom of the scorpion Androctonus mauretanicus mauretanicus. The peptide has been named kaliotoxin (KTX). It is a single 4-kDa polypeptide chain. Its complete amino acid sequence has been determined. KTX displays sequence homology with other scorpion-derived inhibitors of Ca(2+)-activated or voltage-gated K+ channels: 44% homology with charybdotoxin (CTX), 52% with noxiustoxin (NTX), and 44% with iberiotoxin (IbTX). Electrophysiological experiments performed in identified nerve cells from the mollusc Helix pomatia showed that KTX specifically suppressed the whole cell Ca(2+)-activated K+ current. KTX had no detectable effects on voltage-gated K+ current (delayed rectifier and fast transient A current) or on L-type Ca2+ currents. KTX interacts in a one-to-one way with KCa channels with a Kd of 20 nM. Single channel experiments were performed on high conductance KCa channels excised from the above Helix neurons and from rabbit coeliac ganglia sympathetic neurons. KTX acted exclusively at the outer face of the channel. KTX applied on excised outside-out KCa channels induced a transient period of fast-flicker block followed by a persistent channel blockade. The KTX-induced block was not voltage-dependent which suggests differences in the blockade of KCa channels by KTX and by CTX. Comparison of KTX and CTX sequences leads to the identification of a short amino acid sequence (26-33) which may be implicated in the toxin-channel interaction. KTX therefore appears to be a useful tool for elucidating the molecular pharmacology of the high conductance Ca(2+)-activated K+ channel.

10.1016/s0021-9258(18)45993-5

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Citations (192)

Characterization of PO₁, a new peptide ligand of the apamin‐sensitive Ca²⁺ activated K⁺ channel

International journal of peptide & protein research (1996)

H. Zerrouk Fatima Laraba‐Djebari Valérie Frémont Abdel‐Raheim M.A. Meki H. Darbon

A new peptide ligand of the small conductance Ca 2+ activated K + channels has been purified from the venom (obtained by manual rather than electrical stimulation of the scorpion Androctonus mauretanicus mauretanicus ), by following the inhibition of the 125 I‐apamin binding to its receptor on rat brain synaptosomes. Only one step on a C 18 reversed‐phase high‐performance liquid chromatography column was necessary to obtain PO1. Its K 0.5 for the apamin binding site was 100 nM. The amino acid sequence of PO1 is different from those of leiurotoxin and PO5. For the first time the same peptide was also purified from the venoms of two other species of North African scorpions, Androctonus austmlis and Buthus occitanus tunetanus . PO1 was chemically synthesized by the solid‐phase technique and fully characterized. A model of PO1 was constructed by amino acid replacement using PO5 nuclear magnetic resonance studies as the starting model. Structure‐activity relationships between these toxins and their receptor are discussed.

Apamin

10.1111/j.1399-3011.1996.tb00870.x

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Citations (45)

Analysis by high-performance liquid chromatography of Androctonus mauretanicus mauretanicus (black scorpion) venom

H. Zerrouk Pierre E. Bougis Brigitte Céard A. Benslimane Marie‐France Martin‐Eauclaire

Scorpion Venoms

10.1016/0041-0101(91)90078-6

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Citations (34)

Structure activity relationship studies on kaliotoxin, a peptidic K+ channel blocker

Peptides (1994)

J. Van Rietschoten R. Romi Marcel Crest F. Sampiéri H. Zerrouk

Channel blocker

10.1007/978-94-011-0683-2_175

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Citations (0)