Imre Berger: Decoding Echis Viper Venom Proteins in the Lab
Imre Berger, Founding Director of Max Planck Centre for Minimal Biology at University of Bristol, shared a post on LinkedIn about a recent article he and his colleagues co-authored, published in Toxins, adding:
“Today’s news comes with a bite!
Snake venom is scary stuff…
But in deadly venoms are some fascinating proteins with remarkable biological properties.
In our latest paper, we take a closer look at Echis viper disintegrins – tiny venom proteins that can interfere with blood platelet aggregation and cell migration.
The surprising bit?
Small changes within just three amino acids – and their molecular surroundings – result in very different tricks!
We produced these venom proteins recombinantly (no snakes harmed), analysed their activities and showed that our laboratory-made versions faithfully reproduce the activity of their natural counterparts.
And now we can get plenty, and no need to chase the vipers…(ever tried?).
Science is a team sport – fantastic and fun international collaborations with Liverpool, Liège, Marseille.
Congratulations to our Iara Cardoso, who spearheaded this work, and all co-authors for their contributions.”
Title: Recombinant Echis Disintegrins Reveal Distinct Inhibitory Profiles on Human Platelet Aggregation and Endothelial Cell Migration
Authors: Iara A. Cardoso, Sophie Hall, Thomas Crasset, Mark C. Wilkinson, Adam Robinson, Bronwyn Rand, Dakang Shen, Connor E. Webb, Richard Stenner, David K. T. Waterhouse, Ingeborg Hers, Renaud Vincentelli, Imre Berger, Nicholas R. Casewell, Loïc Quinton, Alastair W. Poole, Christiane Schaffitzel
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