Applied and Environmental Microbiology · 2000 · 117 citations · 22 references
Life SciencesEntomologyMicrobiologyInsect GeneticsMicrobial GeneticsProtein EngineeringBacterial ToxinsToxin-mediated PathogenesisBacterial Insecticidal ToxinsCry ProteinsDomain - Domain InteractionsDomain-domain InteractionsInsect Defense MechanismsInsect Resistance To Bacterial ToxinsNovel Insecticidal ProteinsToxin Function
In order to test our hypothesis that Bacillus thuringiensis delta-endotoxin Cry1Ca domain III functions as a determinant of specificity for Spodoptera exigua, regardless of the origins of domains I and II, we have constructed by cloning and in vivo recombination a collection of hybrid proteins containing domains I and II of various Cry1 toxins combined with domain III of Cry1Ca. Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ea, and Cry1Fa all become more active against S. exigua when their domain III is replaced by (part of) that of Cry1Ca. This result shows that domain III of Cry1Ca is an important and versatile determinant of S. exigua specificity. The toxicity of the hybrids varied by a factor of 40, indicating that domain I and/or II modulate the activity as well. Cry1Da-Cry1Ca hybrids were an exception in that they were not significantly active against S. exigua or Manduca sexta, whereas both parental proteins were highly toxic. Incidentally, in a Cry1Ba-Cry1Ca hybrid, Cry1Ca domain III can also strongly increase toxicity for M. sexta.
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Jeroen Van Rie, Stefan Jansens, Herman Höfte et al. · Applied and Environmental Microbiology · 1990 · 358 citations · Full text
Specificity of <i>Bacillus thuringiensis</i>δ‐endotoxins
Jeroen Van Rie, Stefan Jansens, Herman Höfte et al. · European Journal of Biochemistry · 1989 · 345 citations