Mutations at the arginine residues in α8 loop of Bacillus thuringiensis δ‐endotoxin Cry1Ac affect toxicity and binding to Manduca sexta and Lymantria dispar aminopeptidase N

FEBS Letters

Adang, Michael J.³  Son, Joo J.²  Lee, Mi Kyong²  You, Taek H.²  Curtiss, April²  Jenkins, Jeremy L.¹  Dean, Donald H.² 

[1] Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA;Department of Biochemistry, The Ohio State University, 484 W. 12th Ave., Columbus, OH 43210, USA;Department of Entomology, University of Georgia, Athens, GA 30602-2603, USA

关键词: Brush border membrane vesicle;    Aminopeptidase N;    Surface plasmon resonance;    Bacillus thuringiensis;    Lymantria dispar;    Manduca sexta;   

DOI  :  10.1016/S0014-5793(01)02446-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The functional role of the α8 loop residues in domain II of Bacillus thuringiensis Cry1Ac toxin was examined. Alanine substitution mutations were introduced in the residues from 275 to 293. Among the mutant toxins, substitutions at R281 and R289 affected toxicity to Manduca sexta and Lymantria dispar. Loss of toxicity by these mutant toxins was well correlated with reductions in binding affinity for brush border membrane vesicles and the purified receptor, aminopeptidase N (APN), from both insects. These data suggest that the two arginine residues in the α8 loop region are important in toxicity and APN binding in L. dispar and M. sexta.

【 授权许可】

Unknown