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Interaction between functional domains of Bacillus thuringiensis insecticidal crystal proteins.
- Source :
-
Applied and environmental microbiology [Appl Environ Microbiol] 1999 Jul; Vol. 65 (7), pp. 2918-25. - Publication Year :
- 1999
-
Abstract
- Interactions among the three structural domains of Bacillus thuringiensis Cry1 toxins were investigated by functional analysis of chimeric proteins. Hybrid genes were prepared by exchanging the regions coding for either domain I or domain III among Cry1Ab, Cry1Ac, Cry1C, and Cry1E. The activity of the purified trypsin-activated chimeric toxins was evaluated by testing their effects on the viability and plasma membrane permeability of Sf9 cells. Among the parental toxins, only Cry1C was active against these cells and only chimeras possessing domain II from Cry1C were functional. Combination of domain I from Cry1E with domains II and III from Cry1C, however, resulted in an inactive toxin, indicating that domain II from an active toxin is necessary, but not sufficient, for activity. Pores formed by chimeric toxins in which domain I was from Cry1Ab or Cry1Ac were slightly smaller than those formed by toxins in which domain I was from Cry1C. The properties of the pores formed by the chimeras are therefore likely to result from an interaction between domain I and domain II or III. Domain III appears to modulate the activity of the chimeric toxins: combination of domain III from Cry1Ab with domains I and II of Cry1C gave a protein which was more strongly active than Cry1C.
- Subjects :
- Animals
Bacillus thuringiensis chemistry
Bacillus thuringiensis growth & development
Bacillus thuringiensis Toxins
Bacterial Proteins metabolism
Bacterial Proteins pharmacology
Cells, Cultured
Electroporation
Endotoxins metabolism
Endotoxins pharmacology
Hemolysin Proteins
Inclusion Bodies
Insecticides
Microscopy, Video
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Recombinant Fusion Proteins pharmacology
Spodoptera
Bacillus thuringiensis metabolism
Bacterial Proteins chemistry
Bacterial Toxins
Cell Membrane Permeability drug effects
Endotoxins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0099-2240
- Volume :
- 65
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Applied and environmental microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 10388684
- Full Text :
- https://doi.org/10.1128/AEM.65.7.2918-2925.1999