Open AccessDisplay of Biologically Functional Insecticidal Toxin on the Surface of λ Phage
Author(s) -
Susana Vı́lchez,
Juliette Jacoby,
David J. Ellar
Publication year - 2004
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.70.11.6587-6594.2004
Subject(s) - bacillus thuringiensis , phage display , biology , bacteriophage , toxin , diamondback moth , protein engineering , cry1ac , capsid , computational biology , microbiology and biotechnology , genetically modified crops , gene , biochemistry , genetics , bacteria , escherichia coli , transgene , lepidoptera genitalia , botany , antibody , plutella , enzyme
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.