Cloning of a prothrombin activator-like metalloproteinase from the West African saw-scaled viper, Echis ocellatus

S. S. Hasson, R. D G Theakston, R. A. Harrison

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Systemic envenoming by the saw-scaled viper, Echis ocellatus, is responsible for more deaths than any other snake in West Africa. Despite its medical importance, there have been few investigations into the toxin composition of the venom of this viper. Here we describe the isolation of E. ocellatus venom gland cDNAs encoding a protein of 514 amino acids that showed 91% sequence similarity to Ecarin, a prothrombin-activating metalloproteinase from the venom of the East African viper, E. pyramidum leakeyi, that induces severe consumption coagulopathy. Structural similarities between the E. ocellatus metalloproteinase and analogues in venoms of related vipers suggest that antibodies raised to phylogenetically conserved E. ocellatus metalloproteinase domains may have potential for cross-specific and cross-generic neutralisation of analogous venom toxins.

Original languageEnglish
Pages (from-to)629-634
Number of pages6
JournalToxicon
Volume42
Issue number6
DOIs
Publication statusPublished - Nov 2003

Fingerprint

Cloning
Venoms
Metalloproteases
Prothrombin
Viper Venoms
Organism Cloning
Western Africa
Snakes
Disseminated Intravascular Coagulation
Complementary DNA
Amino Acids
Antibodies
Proteins
Chemical analysis

Keywords

  • cDNA cloning
  • Echis ocellatus
  • Prothrombin activator

ASJC Scopus subject areas

  • Toxicology

Cite this

Cloning of a prothrombin activator-like metalloproteinase from the West African saw-scaled viper, Echis ocellatus. / Hasson, S. S.; Theakston, R. D G; Harrison, R. A.

In: Toxicon, Vol. 42, No. 6, 11.2003, p. 629-634.

Research output: Contribution to journalArticle

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