In vivo crystallization of three-domain cry toxins

Adalat, Rooma, Saleem, Faiza, Crickmore, Neil, Naz, Shagufta and Shakoori, Abdul Rauf (2017) In vivo crystallization of three-domain cry toxins. Toxins, 9 (3). a80. ISSN 2072-6651

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Abstract

Bacillus thuringiensis (Bt) is the most successful, environmentally-friendly, and intensively studied microbial insecticide. The major characteristic of Bt is the production of proteinaceous crystals containing toxins with specific activity against many pests including dipteran, lepidopteran, and coleopteran insects, as well as nematodes, protozoa, flukes, and mites. These crystals allow large quantities of the protein toxins to remain stable in the environment until ingested by a susceptible host. It has been previously established that 135 kDa Cry proteins have a crystallization domain at their C-terminal end. In the absence of this domain, Cry proteins often need helper proteins or other factors for crystallization. In this review, we classify the Cry proteins based on their requirements for crystallization.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Q Science > QR Microbiology
Q Science > QR Microbiology > QR0075 Bacteria
Depositing User: Neil Crickmore
Date Deposited: 14 Mar 2017 10:28
Last Modified: 14 Mar 2017 10:34
URI: http://sro.sussex.ac.uk/id/eprint/67078

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