Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom

TB Chen, R Folan, HF Kwok, EJ O'Kane, AJ Bjourson, C Shaw

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The venoms of buthid scorpions are known to contain basic, single-chain protein toxins (alpha toxins) consisting of 60-70 amino acid residues that are tightly folded by four disulfide bridges. Here we describe isolation and sequencing of three novel putative alpha toxins (AamH1-3) from the venom of the North African scorpion, Androctonus amoreuxi, and subsequent cloning of their precursor cDNAs from the same sample of venom. This experimental approach can expedite functional genomic analyses of the protein toxins from this group of venomous animals and does not require specimen sacrifice for cloning of protein toxin precursor cDNAs. (C) 2003 Elsevier Science B.V. All rights reserved.
LanguageEnglish
Pages115-121
JournalRegulatory Peptides
Volume115
Issue number2
DOIs
Publication statusPublished - Sep 2003

Fingerprint

Androctonus
neurotoxins
Scorpiones
venoms
toxins
sampling
proteins
sulfides
genomics
amino acids

Cite this

@article{fd2d5d95ce894c378c9c2516b94e3532,
title = "Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom",
abstract = "The venoms of buthid scorpions are known to contain basic, single-chain protein toxins (alpha toxins) consisting of 60-70 amino acid residues that are tightly folded by four disulfide bridges. Here we describe isolation and sequencing of three novel putative alpha toxins (AamH1-3) from the venom of the North African scorpion, Androctonus amoreuxi, and subsequent cloning of their precursor cDNAs from the same sample of venom. This experimental approach can expedite functional genomic analyses of the protein toxins from this group of venomous animals and does not require specimen sacrifice for cloning of protein toxin precursor cDNAs. (C) 2003 Elsevier Science B.V. All rights reserved.",
author = "TB Chen and R Folan and HF Kwok and EJ O'Kane and AJ Bjourson and C Shaw",
year = "2003",
month = "9",
doi = "10.1016/S0167-0115(03)00146-0",
language = "English",
volume = "115",
pages = "115--121",
journal = "Regulatory Peptides",
issn = "0167-0115",
publisher = "Elsevier",
number = "2",

}

Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom. / Chen, TB; Folan, R; Kwok, HF; O'Kane, EJ; Bjourson, AJ; Shaw, C.

In: Regulatory Peptides, Vol. 115, No. 2, 09.2003, p. 115-121.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom

AU - Chen, TB

AU - Folan, R

AU - Kwok, HF

AU - O'Kane, EJ

AU - Bjourson, AJ

AU - Shaw, C

PY - 2003/9

Y1 - 2003/9

N2 - The venoms of buthid scorpions are known to contain basic, single-chain protein toxins (alpha toxins) consisting of 60-70 amino acid residues that are tightly folded by four disulfide bridges. Here we describe isolation and sequencing of three novel putative alpha toxins (AamH1-3) from the venom of the North African scorpion, Androctonus amoreuxi, and subsequent cloning of their precursor cDNAs from the same sample of venom. This experimental approach can expedite functional genomic analyses of the protein toxins from this group of venomous animals and does not require specimen sacrifice for cloning of protein toxin precursor cDNAs. (C) 2003 Elsevier Science B.V. All rights reserved.

AB - The venoms of buthid scorpions are known to contain basic, single-chain protein toxins (alpha toxins) consisting of 60-70 amino acid residues that are tightly folded by four disulfide bridges. Here we describe isolation and sequencing of three novel putative alpha toxins (AamH1-3) from the venom of the North African scorpion, Androctonus amoreuxi, and subsequent cloning of their precursor cDNAs from the same sample of venom. This experimental approach can expedite functional genomic analyses of the protein toxins from this group of venomous animals and does not require specimen sacrifice for cloning of protein toxin precursor cDNAs. (C) 2003 Elsevier Science B.V. All rights reserved.

U2 - 10.1016/S0167-0115(03)00146-0

DO - 10.1016/S0167-0115(03)00146-0

M3 - Article

VL - 115

SP - 115

EP - 121

JO - Regulatory Peptides

T2 - Regulatory Peptides

JF - Regulatory Peptides

SN - 0167-0115

IS - 2

ER -