Bacterial expression of a snake venom metalloproteinase inhibitory protein from the North American opossum (D.virginiana).

摘要: Abstract A variety of opossum species are resistant to snake venoms due the presence antihemorrhagic and antimyotoxic acidic serum glycoproteins that inhibit several toxic venom components. Two virtually identical proteins isolated from either North American (D. virginiana) or South big-eared aurita), termed oprin DM43 respectively, specific metalloproteinases (SVMPs). better understanding structure these may provide useful insight determine their mechanism action for development therapeutics against global health concern snake-bite envenomation. The aim this work is produce a recombinant metalloproteinase inhibitor (SVMPI) similar above in Escherichia coli if bacterially produced protein inhibits proteolytic properties Western Diamondback rattlesnake (C. atrox) venom. resulting heterologous SVMPI was with 6-Histidine maltose binding (MBP) affinity tag on C-terminus N-terminus protein, respectively. solubility enhancing MBP resulted significantly more soluble expression. inhibitory activity measured using two complementary assays labeled showed 7-fold less as compared SVMPI. Thus, derived an unlabeled high (IC50 = 4.5 μM). use fusion construct appears be productive way express sufficient quantities mammalian E. further study.