In Vivo Crystallization of Three-Domain Cry Toxins

Toxins (Basel). 2017 Mar 9;9(3):80. doi: 10.3390/toxins9030080.

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.

Keywords: Bacillus thuringiensis; C terminal domain; helper protein.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis / genetics
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallization
  • Endotoxins / chemistry*
  • Endotoxins / genetics
  • Hemolysin Proteins / chemistry*
  • Hemolysin Proteins / genetics
  • Humans
  • Protein Domains

Substances

  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins