JBC Transcription and Nuclear Factor Monoclonals

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J. Biol. Chem., Vol. 265, Issue 4, 2054-2059, 02, 1990

Curtatoxins. Neurotoxic insecticidal polypeptides isolated from the funnel-web spider Hololena curta

A Stapleton, DT Blankenship, BL Ackermann, TM Chen, GW Gorder, GD Manley, MG Palfreyman, JE Coutant and AD Cardin
Merrell Dow Research Institute, Cincinnati, Ohio 45215.

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.
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