toxins-09-00080.pdf (797.96 kB)
In vivo crystallization of three-domain cry toxins
journal contribution
posted on 2023-06-09, 05:27 authored by Rooma Adalat, Faiza Saleem, Neil CrickmoreNeil Crickmore, Shagufta Naz, Abdul Rauf ShakooriBacillus 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.
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Publication status
- Published
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- Published version
Journal
ToxinsISSN
2072-6651Publisher
Multidisciplinary Digital Publishing InstituteExternal DOI
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3Volume
9Article number
a80Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2017-03-14First Open Access (FOA) Date
2017-03-14First Compliant Deposit (FCD) Date
2017-03-14Usage metrics
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