Curtatoxins: neurotoxic insecticidal polypeptides isolated from the funnel-web spider Hololena curta

Three polypeptide neurotoxins (curtatoxins) were isolated from the venom of the spider Hololena curta by reverse-phase high performance liquid chromatography, gel permeation, and ion-exchange chromatography. The purified toxins induced an immediate paralysis in the cricket Acheta domestica that resu...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 265; no. 4; pp. 2054 - 2059
Main Authors:	Stapleton, A. (Merrell Dow Research Institute, Cincinnati, OH), Blankenship, D.T, Ackermann, B.L, Chen, T.M, Gorder, G.W, Manley, G.D, Palfreyman, M.G, Coutant, J.E, Cardin, A.D
Format:	Journal Article
Language:	English
Published:	Bethesda, MD American Society for Biochemistry and Molecular Biology 05-02-1990
Subjects:	Agatoxins Agelenidae Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals ARACHNIDA Araneae Biological and medical sciences Chromatography, Gel Chromatography, High Pressure Liquid Chromatography, Ion Exchange curtatoxins Fundamental and applied biological sciences. Psychology Gryllidae Hololena curta INSECTICIDAS INSECTICIDE INSECTICIDES Lethal Dose 50 Molecular Sequence Data NERVOUS SYSTEM Neuropeptides - isolation & purification Neuropeptides - toxicity Neurotoxins - isolation & purification PEPTIDE PEPTIDES PEPTIDOS Protein Conformation Proteins SISTEMA NERVIOSO Spiders Structure-Activity Relationship SYSTEME NERVEUX TOXINAS TOXINE TOXINS VENENO DE SERPIENTES VENIN venom VENOMS Arachnida Insecticide Polypeptide Arthropoda Edman degradation Neurotoxin HPLC chromatography Invertebrata Biological activity Aminoacid sequence Structural analysis
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Summary:	Three polypeptide neurotoxins (curtatoxins) were isolated from the venom of the spider Hololena curta by reverse-phase high performance liquid chromatography, gel permeation, and ion-exchange chromatography. The purified toxins induced an immediate paralysis in the cricket Acheta domestica that resulted in desiccation and death of the insect within 24-48 h (LD50 congruent to 4-20 micrograms/g); this toxic effect is consistent with irreversible presynaptic neuromuscular blockade. Curtatoxins are a class of sequence-related, cysteine-rich, carboxyl-terminal amidated polypeptides of 36 to 38 amino acid residues. The cysteine residues are conserved at identical sequence positions among these polypeptides and form 4 intramolecular disulfide bonds. Hydropathy calculations show that the toxins have an internal hydrophobic region flanked by hydrophilic and oppositely charged amino- and carboxyl-terminal ends. By analogy to other cysteine-rich arthropod venom proteins, the folded structure of the curtatoxins is likely important for their target specificity and mode of action at the neuromuscular junction.
Bibliography:	H01 9025060 L50 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(19)39939-9