20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances yield, crystal size and solubility of Cry3A
Aims: To determine whether the 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of the Cry3A coleopteran toxin and whether the crystalline inclusions produced are toxic to neonates of the Colorado potato beetle, Leptinotarsa...
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Published in | Letters in applied microbiology Vol. 54; no. 2; pp. 88 - 95 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Oxford, UK
Blackwell Publishing Ltd
01.02.2012
Blackwell |
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Abstract | Aims: To determine whether the 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of the Cry3A coleopteran toxin and whether the crystalline inclusions produced are toxic to neonates of the Colorado potato beetle, Leptinotarsa decemlineata. Methods and Results: The cry3A gene was expressed in the 4Q7 strain of B. thuringiensis ssp. israelensis in the absence or presence of the 20‐kDa gene. The 20‐kDa protein enhanced Cry3A yield by 2·7‐fold per unit of fermentation medium. Crystal volumes averaged 2·123 and 0·964 μm3 when synthesized in, respectively, the presence or absence of the 20‐kDa protein. Both crystals were soluble at pH 5 and pH 6; however, the larger crystal was 1·7× and 1·5× more soluble at, respectively, pH 7 and pH 10. No significant difference in toxicity against L. decemlineata neonates was observed. Conclusions: This report demonstrated that the 20‐kDa chaperone‐like protein enhances yield, volume and solubility of the coleopteran Cry3A crystalline inclusions per unit crystal/spore mixture. Significance and Impact of the Study: This is the first report showing that an accessory protein (20‐kDa) could enhance synthesis and crystallization of Cry3A, a finding that could be beneficial for commercial production of this coleopteran‐specific insecticidal protein for microbial insecticides and possibly even for transgenic crops. |
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AbstractList | Aims: To determine whether the 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of the Cry3A coleopteran toxin and whether the crystalline inclusions produced are toxic to neonates of the Colorado potato beetle, Leptinotarsa decemlineata.
Methods and Results: The cry3A gene was expressed in the 4Q7 strain of B. thuringiensis ssp. israelensis in the absence or presence of the 20‐kDa gene. The 20‐kDa protein enhanced Cry3A yield by 2·7‐fold per unit of fermentation medium. Crystal volumes averaged 2·123 and 0·964 μm3 when synthesized in, respectively, the presence or absence of the 20‐kDa protein. Both crystals were soluble at pH 5 and pH 6; however, the larger crystal was 1·7× and 1·5× more soluble at, respectively, pH 7 and pH 10. No significant difference in toxicity against L. decemlineata neonates was observed.
Conclusions: This report demonstrated that the 20‐kDa chaperone‐like protein enhances yield, volume and solubility of the coleopteran Cry3A crystalline inclusions per unit crystal/spore mixture.
Significance and Impact of the Study: This is the first report showing that an accessory protein (20‐kDa) could enhance synthesis and crystallization of Cry3A, a finding that could be beneficial for commercial production of this coleopteran‐specific insecticidal protein for microbial insecticides and possibly even for transgenic crops. To determine whether the 20-kDa chaperone-like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of the Cry3A coleopteran toxin and whether the crystalline inclusions produced are toxic to neonates of the Colorado potato beetle, Leptinotarsa decemlineata. The cry3A gene was expressed in the 4Q7 strain of B. thuringiensis ssp. israelensis in the absence or presence of the 20-kDa gene. The 20-kDa protein enhanced Cry3A yield by 2·7-fold per unit of fermentation medium. Crystal volumes averaged 2·123 and 0·964 μm(3) when synthesized in, respectively, the presence or absence of the 20-kDa protein. Both crystals were soluble at pH 5 and pH 6; however, the larger crystal was 1·7× and 1·5× more soluble at, respectively, pH 7 and pH 10. No significant difference in toxicity against L. decemlineata neonates was observed. This report demonstrated that the 20-kDa chaperone-like protein enhances yield, volume and solubility of the coleopteran Cry3A crystalline inclusions per unit crystal/spore mixture. This is the first report showing that an accessory protein (20-kDa) could enhance synthesis and crystallization of Cry3A, a finding that could be beneficial for commercial production of this coleopteran-specific insecticidal protein for microbial insecticides and possibly even for transgenic crops. Aims: To determine whether the 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of the Cry3A coleopteran toxin and whether the crystalline inclusions produced are toxic to neonates of the Colorado potato beetle, Leptinotarsa decemlineata. Methods and Results: The cry3A gene was expressed in the 4Q7 strain of B. thuringiensis ssp. israelensis in the absence or presence of the 20‐kDa gene. The 20‐kDa protein enhanced Cry3A yield by 2·7‐fold per unit of fermentation medium. Crystal volumes averaged 2·123 and 0·964 μm3 when synthesized in, respectively, the presence or absence of the 20‐kDa protein. Both crystals were soluble at pH 5 and pH 6; however, the larger crystal was 1·7× and 1·5× more soluble at, respectively, pH 7 and pH 10. No significant difference in toxicity against L. decemlineata neonates was observed. Conclusions: This report demonstrated that the 20‐kDa chaperone‐like protein enhances yield, volume and solubility of the coleopteran Cry3A crystalline inclusions per unit crystal/spore mixture. Significance and Impact of the Study: This is the first report showing that an accessory protein (20‐kDa) could enhance synthesis and crystallization of Cry3A, a finding that could be beneficial for commercial production of this coleopteran‐specific insecticidal protein for microbial insecticides and possibly even for transgenic crops. |
Author | Bideshi, D.K Ortego, F Federici, B.A Farinós, G.P Diaz‐Mendoza, M |
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Keywords | 20-kDa protein Chrysomelidae chaperone-like protein Coleoptera Applied microbiology Insecta Bacillus thuringiensis Chaperone Crystals Solubility Bacillaceae Protein Bacillales Leptinotarsa decemlineata Colorado potato beetle Arthropoda Bacteria Yield Biopesticide Invertebrata Cry3A Microbial insecticide |
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Snippet | Aims: To determine whether the 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of... Aims: To determine whether the 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of... To determine whether the 20-kDa chaperone-like protein of Bacillus thuringiensis ssp. israelensis enhances synthesis, crystallization and solubility of the... |
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SubjectTerms | 20-kDa protein Animals Bacillus thuringiensis Bacillus thuringiensis - chemistry Bacillus thuringiensis - genetics Bacillus thuringiensis - metabolism Bacillus thuringiensis subsp. israelensis Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacterial Proteins - ultrastructure Biological and medical sciences chaperone-like protein Coleoptera - microbiology Colorado Colorado potato beetle Cry3A crystallization crystals Endotoxins - chemistry Endotoxins - genetics Endotoxins - metabolism fermentation Fundamental and applied biological sciences. Psychology genes Hemolysin Proteins - chemistry Hemolysin Proteins - genetics Hemolysin Proteins - metabolism Hemolysin Proteins - ultrastructure Larva - microbiology Leptinotarsa decemlineata microbial insecticides Microbiology Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism neonates Pest Control, Biological Solubility spores Spores, Bacterial - physiology toxicity transgenic plants |
Title | 20‐kDa chaperone‐like protein of Bacillus thuringiensis ssp. israelensis enhances yield, crystal size and solubility of Cry3A |
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