A glycoprotein from a folk medicinal plant, Withania somnifera, inhibits hyaluronidase activity of snake venoms

Comp Biochem Physiol C Toxicol Pharmacol. 2006 Jun;143(2):158-61. doi: 10.1016/j.cbpc.2006.01.006. Epub 2006 Mar 2.

Abstract

Venom hyaluronidases help in rapid spreading of the toxins by destroying the integrity of the extra-cellular matrix of the tissues in the victims. A hyaluronidase inhibitor (WSG) is purified from a folk medicinal plant, Withania somnifera. The glycoprotein inhibited the hyaluronidase activity of cobra (Naja naja) and viper (Daboia russelii) venoms, which was demonstrated by zymogram assay and staining of the skin tissues for differential activity. WSG completely inhibited the activity of the enzyme at a concentration of 1:1 w/w of venom to WSG. Thus we are able to demonstrate that the glycoprotein inhibits hyaluronidase activity of the venoms. External application of the plant extract as an antidote in rural parts of India to snakebite victims appears to have a scientific basis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antivenins / isolation & purification
  • Antivenins / pharmacology*
  • Elapid Venoms / enzymology*
  • Elapid Venoms / toxicity
  • Elapidae*
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology
  • Glycoproteins / isolation & purification
  • Glycoproteins / pharmacology*
  • Humans
  • Hyaluronic Acid / metabolism
  • Hyaluronoglucosaminidase / antagonists & inhibitors*
  • Hyaluronoglucosaminidase / metabolism
  • In Vitro Techniques
  • Plants, Medicinal
  • Russell's Viper*
  • Skin / drug effects
  • Skin / metabolism
  • Viper Venoms / enzymology*
  • Viper Venoms / toxicity
  • Withania / chemistry*

Substances

  • Antivenins
  • Elapid Venoms
  • Enzyme Inhibitors
  • Glycoproteins
  • Viper Venoms
  • Hyaluronic Acid
  • Hyaluronoglucosaminidase