Purification, cloning and characterization of a metalloproteinase from Naja atra venom
Toxicon, ISSN: 0041-0101, Vol: 56, Issue: 8, Page: 1459-1469
2010
- 42Citations
- 38Captures
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Metrics Details
- Citations42
- Citation Indexes42
- 42
- CrossRef33
- Captures38
- Readers38
- 38
Article Description
The complement system is a very important part of the immune system. Many snake venoms possess activities that influence the complement. A new metalloproteinase (termed atrase B) with anticomplementary activity was purified from Naja atra venom. Atrase B is a single chain glycoprotein with a molecular mass of 49.4 kDa and an isoelectric point of 9.7. Its N-terminal sequence shows high homology to those of metalloproteinases from cobra venoms. The cDNA sequence reveals that atrase B is a PIII class metalloproteinase. Atrase B slowly cleaves the Aα chain of fibrinogen. It also exhibits edema-inducing activity, but has no hemorrhagic activity and proteolytic activity against fibrin, azocasein, and N-benzoyl- l -arginine ethyl ester. Interestingly, atrase B inhibits activation of the complement classical and alternative pathways in a dose- and time-dependent manner. Complement components factor B and C6 are major targets for atrase B to cleave. Atrase B is the first identified SVMP that cleaves complement components factor B, C6, C7, and C8.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0041010110003326; http://dx.doi.org/10.1016/j.toxicon.2010.08.013; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77958462138&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/20837040; https://linkinghub.elsevier.com/retrieve/pii/S0041010110003326; https://dx.doi.org/10.1016/j.toxicon.2010.08.013
Elsevier BV
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