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Applied and Environmental Microbiology, July 1999, p. 2918-2925, Vol. 65, No. 7
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Interaction between Functional Domains of Bacillus thuringiensis Insecticidal Crystal Proteins

Cécile Rang,1 Vincent Vachon,2 Ruud A. de Maagd,3 Mario Villalon,2 Jean-Louis Schwartz,2,4 Dirk Bosch,3 Roger Frutos,1 and Raynald Laprade2,*

IGEPAM-PC, CIRAD, 34032 Montpellier Cedex 1, France1; Groupe de Recherche en Transport Membranaire, Université de Montréal, Montreal, Quebec H3C 3J7,2 and Biotechnology Research Institute, National Research Council, Montreal, Quebec H4P 2R2,4 Canada; and Department of Molecular Biology, Center for Plant Breeding and Reproduction Research, 6700 AA Wageningen, The Netherlands3

Received 28 October 1998/Accepted 30 April 1999

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.

* Corresponding author. Mailing address: Groupe de Recherche en Transport Membranaire, Université de Montréal, P.O. Box 6128, Centre Ville Station, Montreal, Quebec H3C 3J7, Canada. Phone: (514) 343-7960. Fax: (514) 343-7146. E-mail: laprader{at}ere.umontreal.ca.

Applied and Environmental Microbiology, July 1999, p. 2918-2925, Vol. 65, No. 7
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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