In Vivo Crystallization of Three-Domain Cry Toxins
AbstractBacillus 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. View Full-Text
A printed edition of this Special Issue is available here.
Share & Cite This Article
Adalat, R.; Saleem, F.; Crickmore, N.; Naz, S.; Shakoori, A.R. In Vivo Crystallization of Three-Domain Cry Toxins. Toxins 2017, 9, 80.
Adalat R, Saleem F, Crickmore N, Naz S, Shakoori AR. In Vivo Crystallization of Three-Domain Cry Toxins. Toxins. 2017; 9(3):80.Chicago/Turabian Style
Adalat, Rooma; Saleem, Faiza; Crickmore, Neil; Naz, Shagufta; Shakoori, Abdul R. 2017. "In Vivo Crystallization of Three-Domain Cry Toxins." Toxins 9, no. 3: 80.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.