Alanine-substituted mutant on Gly373 and Asn375 of Cry1Ai-h-loop 2 causes reduction in both toxicity and binding against Helicoverpa armigera

Cry1Ai-h-loop 2 is a mutant of Cry1Ai constructed by exchanging loop 2 from Cry1Ah protein and shows insecticidal activity against Helicoverpa armigera.The toxicity of Cry1Ai-h-loop 2,in contrast to the very low toxicity of Cry1Ai,is closely associated with the eleven residues in the loop 2 region.T...

Full description

Saved in:
Bibliographic Details
Published inJournal of Integrative Agriculture Vol. 18; no. 5; pp. 1064 - 1071
Main Authors LIU, Yu-xiao, ZHOU, Zi-shan, LIANG, Ge-mei, SONG, Fu-ping, ZHANG, Jie
Format Journal Article
LanguageEnglish
Published State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, P.R.China 01.05.2019
Elsevier
Subjects
Bacillus thuringiensis
binding affinity
Cry1Ai
Domain II-loop2
Helicoverpa armigera
binding affinity
Helicoverpa armigera
Cry1Ai
Bacillus thuringiensis
Domain Ⅱ-loop2
Online AccessGet full text

Cover

More Information
Summary:Cry1Ai-h-loop 2 is a mutant of Cry1Ai constructed by exchanging loop 2 from Cry1Ah protein and shows insecticidal activity against Helicoverpa armigera.The toxicity of Cry1Ai-h-loop 2,in contrast to the very low toxicity of Cry1Ai,is closely associated with the eleven residues in the loop 2 region.To characterize the key sites of loop 2 in Cry1Ai-h-loop 2,alanine-substituted mutants were generated.The toxicity of these mutants against H.armigera indicated that dual-mutant on Gly373 and Asn375 caused a significant decrease in toxic activity.ELISA binding and competition binding assays demonstrated that the reduction of toxicity in the mutant of interest was correlated with decreased binding affinity.
ISSN:2095-3119
2352-3425
DOI:10.1016/S2095-3119(18)61933-1