In vitro neuromuscular activity of 'colubrid' venoms: clinical and evolutionary implications

Toxicon. 2004 Jun 1;43(7):819-27. doi: 10.1016/j.toxicon.2004.03.012.

Abstract

In this study, venoms from species in the Colubrinae, Homalopsinae, Natricinae, Pseudoxyrhophiinae and Psammophiinae snake families were assayed for activity in the chick biventer cervicis skeletal nerve muscle preparation. Boiga dendrophila, Boiga cynodon, Boiga dendrophila gemincincta, Boiga drapiezii, Boiga irregularis, Boiga nigriceps and Telescopus dhara venoms (10 microg/ml) displayed postsynaptic neuromuscular activity as evidenced by inhibition of indirect (0.1 Hz, 0.2 ms, supramaximal V) twitches. Neostigmine (5 microM) reversed the inhibition caused by B. cynodon venom (10 microg/ml) while the inhibitory effects of Psammophis mossambicus venom (10 microg/ml) spontaneously reversed, indicating a reversible mode of action for both venoms. Trimorphodon biscutatus (10 microg/ml) displayed irreversible presynaptic neurotoxic activity. Detectable levels of phospholipase A2 activity were found only in T. biscutatus, T. dhara and P. mossambicus venoms. The results demonstrate a hitherto unsuspected diversity of pharmacological actions in all lineages which may have implications ranging from clinical management of envenomings to venom evolution.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Analysis of Variance
  • Animals
  • Chickens
  • Muscle Contraction / drug effects*
  • Neostigmine / pharmacology
  • Neuromuscular Agents / antagonists & inhibitors
  • Neuromuscular Agents / metabolism
  • Neuromuscular Agents / toxicity*
  • Neuromuscular Junction / drug effects*
  • Phospholipases A / metabolism
  • Phospholipases A2
  • Phylogeny
  • Snake Venoms / antagonists & inhibitors
  • Snake Venoms / metabolism
  • Snake Venoms / toxicity*
  • Snakes*
  • Species Specificity
  • Time Factors

Substances

  • Neuromuscular Agents
  • Snake Venoms
  • Neostigmine
  • Phospholipases A
  • Phospholipases A2