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In vivo crystallization of three-domain cry toxins

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posted on 2023-06-09, 05:27 authored by Rooma Adalat, Faiza Saleem, Neil CrickmoreNeil Crickmore, Shagufta Naz, Abdul Rauf Shakoori
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.

History

Publication status

  • Published

File Version

  • Published version

Journal

Toxins

ISSN

2072-6651

Publisher

Multidisciplinary Digital Publishing Institute

Issue

3

Volume

9

Article number

a80

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2017-03-14

First Open Access (FOA) Date

2017-03-14

First Compliant Deposit (FCD) Date

2017-03-14

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