Isolation of a polypeptide from Phoneutria nigriventer spider venom responsible for the increased vascular permeability in rabbit skin

Toxicon. 1995 Feb;33(2):171-8. doi: 10.1016/0041-0101(94)00148-2.


Fractionation of Phoneutria nigriventer venom by Sephadex G-10 followed by ion-exchange chromatography yields a fraction (fraction XIII) which increases microvascular permeability in rabbit skin in vivo by activating the tissue kallikrein-kinin system. One polypeptide (PNV3) with the ability to increase microvascular permeability in the rabbit skin in vivo was isolated from fraction XIII and biochemically characterized. PNV3 has 132 amino acid residues with a calculated mol. wt of 14,475. This polypeptide showed the following N-terminal sequence: AVFAIQDQPC. Amino acid analysis indicated the presence of six disulfide bridges and a high content of Glx (20%). Pairwise comparison of PNV3 amino acid sequence with 27 other spider venom polypeptides and proteins indicated that PNV3 presents high similarity (60-70%) with other toxins (Tx2.1, Tx2.5 and Tx2.6) isolated from P. nigriventer venom.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Capillary Permeability / drug effects
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Hydrolases / metabolism
  • Peptides / isolation & purification*
  • Rabbits
  • Skin / blood supply*
  • Spider Venoms / chemistry*
  • Spider Venoms / enzymology
  • Spider Venoms / toxicity*


  • Amino Acids
  • Peptides
  • Spider Venoms
  • Peptide Hydrolases
  • tosylarginine methyl ester hydrolase