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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
Author(s) -
Lee Mi Kyong,
Jenkins Jeremy L.,
You Taek H.,
Curtiss April,
Son Joo J.,
Adang Michael J.,
Dean Donald H.
Publication year - 2001
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/s0014-5793(01)02446-2
Subject(s) - manduca sexta , bacillus thuringiensis , lymantria dispar , biology , manduca , biochemistry , aminopeptidase , mutant , cry1ac , brush border , toxicity , toxin , microbiology and biotechnology , vesicle , chemistry , amino acid , lepidoptera genitalia , insect , transgene , bacteria , botany , membrane , genetics , gene , leucine , genetically modified crops , organic chemistry
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 .