Volume 31 Issue 6
Nov.  2010
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PAN Jian-Yi, YU Zhi-Qiang. Isolation and characterization of Hainantoxin-II, a new neurotoxic peptide from the Chinese bird spider (Haplopelma hainanum). Zoological Research, 2010, 31(6): 570-574. doi: 10.3724/SP.J.1141.2010.06570
Citation: PAN Jian-Yi, YU Zhi-Qiang. Isolation and characterization of Hainantoxin-II, a new neurotoxic peptide from the Chinese bird spider (Haplopelma hainanum). Zoological Research, 2010, 31(6): 570-574. doi: 10.3724/SP.J.1141.2010.06570

Isolation and characterization of Hainantoxin-II, a new neurotoxic peptide from the Chinese bird spider (Haplopelma hainanum)

doi: 10.3724/SP.J.1141.2010.06570
Funds:  This work was supported by the Research Project of the Education Department of Zhejiang Province, China (Y200805989)
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  • Author Bio:

    PAN Jian-Yi

  • Corresponding author: PAN Jian-Yi
  • Received Date: 2010-06-04
  • Rev Recd Date: 2010-10-19
  • Publish Date: 2010-12-22
  • Hainantoxin-II (HnTx-II), a novel neurotoxin, was isolated from the venom of the Chinese bird spider (Haplopelma hainanum) by cation exchange chromatography and reverse-phase HPLC. The toxin was a single chain polypeptide with calculated molecular weight of 4 253.135 obtained by mass spectrometry. The complete amino acid sequence of HnTx-II was determined by Edman degradation and found to contain 37 residues with three disulfide bonds. Results showed HnTx-II can reversibly paralyze cockroaches for several hours after intra-abdominal injection with ED50 of 16 μg/g and kill the insects immediately at a dose of 60 μg/g. It was also shown to kill mice at a LD50 value of 1.41μg/g after intracerebroventricular injection. Hainantoxin-II shares 91% sequence homology with Huwentoxin-II (HwTx-II), an insecticidal peptide from another bird spider(Haplopelma schmidti) with a unique scaffold. While HnTx-II and HwTx-II both exhibit toxic activities in insects and mammals, HnTx-II shows higher insecticidal activity and lower lethiferous activity of mammals than HwTx-II. These results help clarify structural-functional relationships ofthe polypeptide toxin.
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