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A recombinant snake neurotoxin generated by chemical cleavage of a hybrid protein recovers full biological properties
Author(s) -
Boyot Philippe,
Pillet Laurence,
Ducancel Frédéric,
Boulain Jean-Claude,
Tremeau Odile,
Ménez André
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81513-n
Subject(s) - neurotoxin , toxin , cyanogen bromide , recombinant dna , chemistry , protein engineering , nicotinic acetylcholine receptor , biochemistry , acetylcholine receptor , vinyl bromide , cleavage (geology) , receptor , biology , peptide sequence , enzyme , organic chemistry , gene , paleontology , fracture (geology)
We previously reported the production of a fused snake neurotoxin composed of protein A and erabutoxin a in 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.