Premium
Hemorrhagic metalloproteinase, Cc HSM‐III, isolated from Cerastes cerastes venom: Purification and biochemical characterization
Author(s) -
Tachoua Wafa,
BoukhalfaAbib Hinda,
LarabaDjebari Fatima
Publication year - 2017
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21899
Subject(s) - venom , snake venom , viperidae , metalloproteinase , disintegrin , matrix metalloproteinase , envenomation , chemistry , biochemistry , viper venoms , microbiology and biotechnology , biology
Abstract Snake venom metalloproteinases are the most abundant toxins in Viperidae venoms. In this study, a new hemorrhagin, Cc HSM‐III (66 kDa), was purified from Cerastes cerastes venom by gel filtration, ion exchange, and reversed‐phase high‐performance liquid chromatographies. The analysis of Cc HSM‐III by liquid chromatography with a tandem mass spectrometry revealed 32 peptides sharing a homology with P‐III metalloproteinases from Echis ocellatus snake venom. Cc HSM‐III displays hemorrhagic activity with a minimal hemorrhagic dose of 5 μg, which is abolished by ethylene diamine tetracetic acid but not by phenylmethylsulfonyl fluoride. The mechanism underlying Cc HSM‐III hemorrhagic activity is probably due to its extensive proteolytic activity against type IV collagen. Cc HSM‐III induces local tissue damage and an inflammatory response by upregulating both matrix metalloproteinase 2 and 9 in skin of mice. Thus, Cc HSM‐III may play a key role in the pathogenesis of C. cerastes envenomation.