Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels

Elba Villegas; Satomi Adachi-Akahane; Frank Bosmans; Jan Tytgat; Terumi Nakajima; Gerardo Corzo

doi:10.1016/j.toxicon.2008.05.019

Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels

Elba Villegas, Satomi Adachi-Akahane, Frank Bosmans, Jan Tytgat, Terumi Nakajima, Gerardo Corzo

School of Medicine

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Oxytoxins (OxyTx1 and OxyTx2) are disulfide-rich peptides isolated from the venom of the spider Oxyopes lineatus that block voltage-sensitive calcium ion channels (VSCCs). OxyTx1 was identified previously and isolated from the related spider Oxyopes kitabensis; however, its pharmacology was unknown. OxyTx1 and OxyTx2 contain 69 and 55 amino acid residues with molecular masses of 8058.2 and 6175.2 Da, respectively. Oxytoxins contain five disulfide bridges, are amidated at their C-terminus, antagonize P/Q-, N- or L-type VSCCs, and have low amino acid identity to known VSCC blockers from arthropod venoms. OxyTx1 is not specific for VSCCs subtypes when compared to the classical P/Q-type blocker ω-AgaIVA, but OxyTx1 has higher paralytic activity towards Spodoptera litura larvae. Because of their structural and biochemical characteristics OxyTx1 and OxyTx2 may represent a new family of insecticidal peptides.

Original language	English (US)
Pages (from-to)	228-236
Number of pages	9
Journal	Toxicon
Volume	52
Issue number	2
DOIs	https://doi.org/10.1016/j.toxicon.2008.05.019
State	Published - Aug 1 2008

Keywords

Calcium
Electrophysiology
Ion channels
Neurotoxin
Spider

ASJC Scopus subject areas

Toxicology

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10.1016/j.toxicon.2008.05.019

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title = "Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels",

abstract = "Oxytoxins (OxyTx1 and OxyTx2) are disulfide-rich peptides isolated from the venom of the spider Oxyopes lineatus that block voltage-sensitive calcium ion channels (VSCCs). OxyTx1 was identified previously and isolated from the related spider Oxyopes kitabensis; however, its pharmacology was unknown. OxyTx1 and OxyTx2 contain 69 and 55 amino acid residues with molecular masses of 8058.2 and 6175.2 Da, respectively. Oxytoxins contain five disulfide bridges, are amidated at their C-terminus, antagonize P/Q-, N- or L-type VSCCs, and have low amino acid identity to known VSCC blockers from arthropod venoms. OxyTx1 is not specific for VSCCs subtypes when compared to the classical P/Q-type blocker ω-AgaIVA, but OxyTx1 has higher paralytic activity towards Spodoptera litura larvae. Because of their structural and biochemical characteristics OxyTx1 and OxyTx2 may represent a new family of insecticidal peptides.",

keywords = "Calcium, Electrophysiology, Ion channels, Neurotoxin, Spider",

author = "Elba Villegas and Satomi Adachi-Akahane and Frank Bosmans and Jan Tytgat and Terumi Nakajima and Gerardo Corzo",

note = "Funding Information: We are grateful to Dr. Mori who generously supplied BHK-N101, BHK-BI and BHK6 cells and to Dr. Snutch who generously supplied the rat brain α 1C subunit (rbCII). Also we are grateful to Dr. Pierre Escoubas as well as Dr. Nicolas Gilles for their advice on mass spectrometry and binding experiments, respectively. We are grateful to Dr. Gurevitz for the gift of scorpion toxins. This work was supported by grants from the Suntory Institute for Bioorganic Research, and DGAPA IN226006 (UNAM) and CONACyT 49773/24968. This work was also supported in part to JT by G.0330.06 (F.W.O.-Vlaanderen), OT-05-64 (K.U.Leuven) and P6/31 (Interuniversity Attraction Poles Programme – Belgian State – Belgian Science Policy). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2008",

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doi = "10.1016/j.toxicon.2008.05.019",

language = "English (US)",

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T1 - Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels

AU - Villegas, Elba

AU - Adachi-Akahane, Satomi

AU - Bosmans, Frank

AU - Tytgat, Jan

AU - Nakajima, Terumi

AU - Corzo, Gerardo

N1 - Funding Information: We are grateful to Dr. Mori who generously supplied BHK-N101, BHK-BI and BHK6 cells and to Dr. Snutch who generously supplied the rat brain α 1C subunit (rbCII). Also we are grateful to Dr. Pierre Escoubas as well as Dr. Nicolas Gilles for their advice on mass spectrometry and binding experiments, respectively. We are grateful to Dr. Gurevitz for the gift of scorpion toxins. This work was supported by grants from the Suntory Institute for Bioorganic Research, and DGAPA IN226006 (UNAM) and CONACyT 49773/24968. This work was also supported in part to JT by G.0330.06 (F.W.O.-Vlaanderen), OT-05-64 (K.U.Leuven) and P6/31 (Interuniversity Attraction Poles Programme – Belgian State – Belgian Science Policy). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2008/8/1

Y1 - 2008/8/1

N2 - Oxytoxins (OxyTx1 and OxyTx2) are disulfide-rich peptides isolated from the venom of the spider Oxyopes lineatus that block voltage-sensitive calcium ion channels (VSCCs). OxyTx1 was identified previously and isolated from the related spider Oxyopes kitabensis; however, its pharmacology was unknown. OxyTx1 and OxyTx2 contain 69 and 55 amino acid residues with molecular masses of 8058.2 and 6175.2 Da, respectively. Oxytoxins contain five disulfide bridges, are amidated at their C-terminus, antagonize P/Q-, N- or L-type VSCCs, and have low amino acid identity to known VSCC blockers from arthropod venoms. OxyTx1 is not specific for VSCCs subtypes when compared to the classical P/Q-type blocker ω-AgaIVA, but OxyTx1 has higher paralytic activity towards Spodoptera litura larvae. Because of their structural and biochemical characteristics OxyTx1 and OxyTx2 may represent a new family of insecticidal peptides.

AB - Oxytoxins (OxyTx1 and OxyTx2) are disulfide-rich peptides isolated from the venom of the spider Oxyopes lineatus that block voltage-sensitive calcium ion channels (VSCCs). OxyTx1 was identified previously and isolated from the related spider Oxyopes kitabensis; however, its pharmacology was unknown. OxyTx1 and OxyTx2 contain 69 and 55 amino acid residues with molecular masses of 8058.2 and 6175.2 Da, respectively. Oxytoxins contain five disulfide bridges, are amidated at their C-terminus, antagonize P/Q-, N- or L-type VSCCs, and have low amino acid identity to known VSCC blockers from arthropod venoms. OxyTx1 is not specific for VSCCs subtypes when compared to the classical P/Q-type blocker ω-AgaIVA, but OxyTx1 has higher paralytic activity towards Spodoptera litura larvae. Because of their structural and biochemical characteristics OxyTx1 and OxyTx2 may represent a new family of insecticidal peptides.

KW - Calcium

KW - Electrophysiology

KW - Ion channels

KW - Neurotoxin

KW - Spider

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DO - 10.1016/j.toxicon.2008.05.019

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AN - SCOPUS:49649104531

SN - 0041-0101

VL - 52

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EP - 236

JO - Toxicon

JF - Toxicon

IS - 2

ER -

Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels

Abstract

Keywords

ASJC Scopus subject areas

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