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

Pharmaceutical and Pharmacological Sciences

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

16 Citations (Scopus)

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 6175.2Da, 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 omega-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
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
Publication status	Published - 1 Aug 2008

Keywords

Amino Acid Sequence
Animals
Calcium Channel Blockers/chemistry
Calcium Channels, N-Type/drug effects
Cell Membrane/drug effects
Cells, Cultured
Circular Dichroism
Cricetinae
Cysteine/chemistry
Dose-Response Relationship, Drug
Insect Proteins/chemistry
Molecular Sequence Data
Neurons/drug effects
Neurotoxins/chemistry
Ovum/drug effects
Patch-Clamp Techniques
Peptides/chemistry
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spider Venoms/chemistry
Spiders/metabolism
Xenopus laevis

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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 6175.2Da, 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 omega-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 = "Amino Acid Sequence, Animals, Calcium Channel Blockers/chemistry, Calcium Channels, N-Type/drug effects, Cell Membrane/drug effects, Cells, Cultured, Circular Dichroism, Cricetinae, Cysteine/chemistry, Dose-Response Relationship, Drug, Insect Proteins/chemistry, Molecular Sequence Data, Neurons/drug effects, Neurotoxins/chemistry, Ovum/drug effects, Patch-Clamp Techniques, Peptides/chemistry, Sequence Alignment, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spider Venoms/chemistry, Spiders/metabolism, Xenopus laevis",

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

year = "2008",

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

language = "English",

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journal = "TOXICON",

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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

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 6175.2Da, 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 omega-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 6175.2Da, 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 omega-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 - Amino Acid Sequence

KW - Animals

KW - Calcium Channel Blockers/chemistry

KW - Calcium Channels, N-Type/drug effects

KW - Cell Membrane/drug effects

KW - Cells, Cultured

KW - Circular Dichroism

KW - Cricetinae

KW - Cysteine/chemistry

KW - Dose-Response Relationship, Drug

KW - Insect Proteins/chemistry

KW - Molecular Sequence Data

KW - Neurons/drug effects

KW - Neurotoxins/chemistry

KW - Ovum/drug effects

KW - Patch-Clamp Techniques

KW - Peptides/chemistry

KW - Sequence Alignment

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

KW - Spider Venoms/chemistry

KW - Spiders/metabolism

KW - Xenopus laevis

U2 - 10.1016/j.toxicon.2008.05.019

DO - 10.1016/j.toxicon.2008.05.019

M3 - Article

C2 - 18606178

SN - 0041-0101

VL - 52

SP - 228

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

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