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Applied and Environmental Microbiology, November 2004, p. 6587-6594, Vol. 70, No. 11
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.11.6587-6594.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Display of Biologically Functional Insecticidal Toxin on the Surface of {lambda} Phage

Susana Vílchez,1 Juliette Jacoby,2 and David J. Ellar1*

Department of Biochemistry,1 Department of Medicine, Cambridge University, Cambridge, United Kingdom2

Received 23 March 2004/ Accepted 22 June 2004

The successful use of Bacillus thuringiensis insecticidal toxins to control agricultural pests could be undermined by the evolution of insect resistance. Under selection pressure in the laboratory, a number of insects have gained resistance to the toxins, and several cases of resistance in the diamondback moth have been reported from the field. The use of protein engineering to develop novel toxins active against resistant insects could offer a solution to this problem. The display of proteins on the surface of phages has been shown to be a powerful technology to search for proteins with new characteristics from combinatorial libraries. However, this potential of phage display to develop Cry toxins with new binding properties and new target specificities has hitherto not been realized because of the failure of displayed Cry toxins to bind their natural receptors. In this work we describe the construction of a display system in which the Cry1Ac toxin is fused to the amino terminus of the capsid protein D of bacteriophage lambda. The resultant phage was viable and infectious, and the displayed toxin interacted successfully with its natural receptor.

* Corresponding author. Mailing address: Department of Biochemistry, Cambridge University, 80 Tennis Court Rd., Cambridge CB2 1GA, United Kingdom. Phone: 44 (0)1223 333651. Fax: 44 (0)1223 766043. E-mail: dje1{at}mole.bio.cam.ac.uk.

Applied and Environmental Microbiology, November 2004, p. 6587-6594, Vol. 70, No. 11
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.11.6587-6594.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Pigott, C. R., King, M. S., Ellar, D. J. (2008). Investigating the Properties of Bacillus thuringiensis Cry Proteins with Novel Loop Replacements Created Using Combinatorial Molecular Biology. Appl. Environ. Microbiol. 74: 3497-3511 [Abstract] [Full Text]  
  • Yang, Y., Wang, L., Gaviria, A., Yuan, Z., Berry, C. (2007). Proteolytic Stability of Insecticidal Toxins Expressed in Recombinant Bacilli. Appl. Environ. Microbiol. 73: 218-225 [Abstract] [Full Text]  


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