Domains of Bacillus thuringiensis crystal proteins involved in insecticidal activity

H.J. Bosch, B. Schipper, H. van der Kleij, R.A. de Maagd, W.J. Stiekema

Research output: Contribution to journalComment/Letter to the editorAcademic

1 Citation (Scopus)

Abstract

The expected increase in application of Bacillus thuringiensis (Bt) in crop protection makes it necessary to anticipate the development of Bt-resistant insects. To safeguard the long-term use of Bt-based insecticides, we studied the mode of action of Bt crystal proteins. CryIA(b), CryIC and CryIE are all toxic to lepidoptera, but each protein has its own specificity profile. In order to identify regions in the proteins involved in insecticidal specificity, hybrids between the genes cryIA(b) cryIC and cryIE were generated. Plasmids were constructed carrying two truncated crystal protein genes. In vivo recombination between these genes resulted in hybrids encoding full-length 140 kDa protoxins. In this manner, sets of CryIA(b)-CryIE, CryIC-CryIE and CryIE-CryIC hybrid proteins were isolated. The analysis of the CryIC-CryIE hybrids showed that domain II is involved in receptor binding, but that domain II of CryIC is not sufficient for the high activity of this protein towards Spodoptera exigua and Mamestra brassicae. Biochemical evidence and insect toxicity assays indicate that all CryIA(b)-CryIE hybrids are malfolded and precipitate as insoluble aggregates
LanguageEnglish
Pages449
JournalBiocontrol Science and Technology
Volume4
Issue number4
DOIs
Publication statusPublished - 1994

Fingerprint

crystal proteins
Bacillus thuringiensis
Mamestra brassicae
insecticidal proteins
insects
Spodoptera exigua
genes
proteins
protein aggregates
plant protection
mechanism of action
plasmids
insecticides
Lepidoptera
toxicity
receptors
assays

Cite this

@article{34a9cdd0c00a4a288829f507489825f2,
title = "Domains of Bacillus thuringiensis crystal proteins involved in insecticidal activity",
abstract = "The expected increase in application of Bacillus thuringiensis (Bt) in crop protection makes it necessary to anticipate the development of Bt-resistant insects. To safeguard the long-term use of Bt-based insecticides, we studied the mode of action of Bt crystal proteins. CryIA(b), CryIC and CryIE are all toxic to lepidoptera, but each protein has its own specificity profile. In order to identify regions in the proteins involved in insecticidal specificity, hybrids between the genes cryIA(b) cryIC and cryIE were generated. Plasmids were constructed carrying two truncated crystal protein genes. In vivo recombination between these genes resulted in hybrids encoding full-length 140 kDa protoxins. In this manner, sets of CryIA(b)-CryIE, CryIC-CryIE and CryIE-CryIC hybrid proteins were isolated. The analysis of the CryIC-CryIE hybrids showed that domain II is involved in receptor binding, but that domain II of CryIC is not sufficient for the high activity of this protein towards Spodoptera exigua and Mamestra brassicae. Biochemical evidence and insect toxicity assays indicate that all CryIA(b)-CryIE hybrids are malfolded and precipitate as insoluble aggregates",
author = "H.J. Bosch and B. Schipper and {van der Kleij}, H. and {de Maagd}, R.A. and W.J. Stiekema",
year = "1994",
doi = "10.1080/09583159409355356",
language = "English",
volume = "4",
pages = "449",
journal = "Biocontrol Science and Technology",
issn = "0958-3157",
publisher = "Taylor & Francis",
number = "4",

}

Domains of Bacillus thuringiensis crystal proteins involved in insecticidal activity. / Bosch, H.J.; Schipper, B.; van der Kleij, H.; de Maagd, R.A.; Stiekema, W.J.

In: Biocontrol Science and Technology, Vol. 4, No. 4, 1994, p. 449.

Research output: Contribution to journalComment/Letter to the editorAcademic

TY - JOUR

T1 - Domains of Bacillus thuringiensis crystal proteins involved in insecticidal activity

AU - Bosch, H.J.

AU - Schipper, B.

AU - van der Kleij, H.

AU - de Maagd, R.A.

AU - Stiekema, W.J.

PY - 1994

Y1 - 1994

N2 - The expected increase in application of Bacillus thuringiensis (Bt) in crop protection makes it necessary to anticipate the development of Bt-resistant insects. To safeguard the long-term use of Bt-based insecticides, we studied the mode of action of Bt crystal proteins. CryIA(b), CryIC and CryIE are all toxic to lepidoptera, but each protein has its own specificity profile. In order to identify regions in the proteins involved in insecticidal specificity, hybrids between the genes cryIA(b) cryIC and cryIE were generated. Plasmids were constructed carrying two truncated crystal protein genes. In vivo recombination between these genes resulted in hybrids encoding full-length 140 kDa protoxins. In this manner, sets of CryIA(b)-CryIE, CryIC-CryIE and CryIE-CryIC hybrid proteins were isolated. The analysis of the CryIC-CryIE hybrids showed that domain II is involved in receptor binding, but that domain II of CryIC is not sufficient for the high activity of this protein towards Spodoptera exigua and Mamestra brassicae. Biochemical evidence and insect toxicity assays indicate that all CryIA(b)-CryIE hybrids are malfolded and precipitate as insoluble aggregates

AB - The expected increase in application of Bacillus thuringiensis (Bt) in crop protection makes it necessary to anticipate the development of Bt-resistant insects. To safeguard the long-term use of Bt-based insecticides, we studied the mode of action of Bt crystal proteins. CryIA(b), CryIC and CryIE are all toxic to lepidoptera, but each protein has its own specificity profile. In order to identify regions in the proteins involved in insecticidal specificity, hybrids between the genes cryIA(b) cryIC and cryIE were generated. Plasmids were constructed carrying two truncated crystal protein genes. In vivo recombination between these genes resulted in hybrids encoding full-length 140 kDa protoxins. In this manner, sets of CryIA(b)-CryIE, CryIC-CryIE and CryIE-CryIC hybrid proteins were isolated. The analysis of the CryIC-CryIE hybrids showed that domain II is involved in receptor binding, but that domain II of CryIC is not sufficient for the high activity of this protein towards Spodoptera exigua and Mamestra brassicae. Biochemical evidence and insect toxicity assays indicate that all CryIA(b)-CryIE hybrids are malfolded and precipitate as insoluble aggregates

U2 - 10.1080/09583159409355356

DO - 10.1080/09583159409355356

M3 - Comment/Letter to the editor

VL - 4

SP - 449

JO - Biocontrol Science and Technology

T2 - Biocontrol Science and Technology

JF - Biocontrol Science and Technology

SN - 0958-3157

IS - 4

ER -