A recombinant snake neurotoxin generated by chemical cleavage of a hybrid protein recovers full biological properties

Autor: Boyot, Philippe, Pillet, Laurence, Ducancel, Frédéric, Boulain, Jean-Claude, Tremeau, Odile, Ménez, André
Zdroj: FEBS Letters; January 1990, Vol. 266 Issue: 1 p87-90, 4p
Abstrakt: We previously reported the production of a fused snake neurotoxin composed of protein A and erabutoxin ain E. coli[1]. The hybrid had much lower toxicity and affinity for the acetylcholine nicotinic receptor than natural erabutoxin. By treating the hybrid with cyanogen bromide we generated a toxin which was purified in a single step by RP-HPLC. This compound, produced in a good yield, recovered all properties of native erabutoxin a, implying that the lower toxic activities of the hybrid were due to the bulky protein A and not to an incorrect folding of the toxin. This work serves as a basis for future studies of toxin-receptor interactions using engineered toxin mutants.
Databáze: Supplemental Index