Ammoditoxins (Atx) are type A2 secretory phospholipases (sPLA2) from the venom of the nose-horned viper (Vipera ammodytes ammodytes) with presynaptic neurotoxicity (β neurotoxicity). Despite many recent discoveries in this field, the underlying mechanism and the role of Atx's enzymatic activity therein remains poorly understood. To gain better insight, researchers have developed an enzymatically inactive recombinant mutant AtxA(D49S). Mutant variant is produced in bacteria, where it aggregates into insoluble inclusion bodies. Thus, it needs to be refolded and purified before use, but the yield of such refolding is usually quite low.
The goal of our work was to improve the refolding yield using a known Atx ligand calmodulin (CaM) as a chaperone. We show that AtxA(D49S) can be successfully refolded using such an approach, however the resulting yield is lower than expected.
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