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

FEBS Letters

Boulain, Jean-Claude¹  Ménez, André¹  Boyot, Philippe¹  Ducancel, Frédéric¹  Pillet, Laurence¹  Tremeau, Odile¹ 

[1] Service de Biochimie, Département de Biologie, Laboratoire d'Ingénierie des Protéines, C.E.N., Saclay, 91191 Gif-sur-Yvette, France

关键词: Snake neurotoxin;    Recombinant protein;    Cyanogen bromide cleavage;    Acetylcholine receptor;   

DOI  :  10.1016/0014-5793(90)81513-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown