Vegetative insecticidal protein enhancing the toxicity of Bacillus thuringiensis subsp kurstaki against Spodoptera exigua

Zhu, Cuizhen; Ruan, Lifang; Peng, Donghai; Zhou, Yu; Sun, Ming

doi:10.1111/j.1472-765x.2005.01817.x

Cited by 50 publications

(29 citation statements)

References 18 publications

(22 reference statements)

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“…Commercial formulations of B. thuringiensis strains contain small amounts of Vip proteins, since these proteins are secreted into the growth medium, which is mostly discarded during the processing of the formulation (81). This problem can be alleviated by directing the expression of the vip3A gene to the sporulation stage by using sporulation-dependent promoters and specific transcription sequences from different cry genes (82)(83)(84)(85). The engineered strains in all these cases showed improved production of Vip3A proteins and higher toxicity to the insects tested.…”

Section: Insecticidal Activitymentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

243

261

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SUMMARYEntomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no sequence similarity to Vip1 or Vip2 and is toxic to a wide variety of members of the Lepidoptera. Its mode of action has been shown to resemble that of the Cry proteins in terms of proteolytic activation, binding to the midgut epithelial membrane, and pore formation, although Vip3A proteins do not share binding sites with Cry proteins. The latter property makes them good candidates to be combined with Cry proteins in transgenic plants (Bacillus thuringiensis-treated crops [Bt crops]) to prevent or delay insect resistance and to broaden the insecticidal spectrum. There are commercially grown varieties of Bt cotton and Bt maize that express the Vip3Aa protein in combination with Cry proteins. For the most recently reported Vip4 family, no target insects have been found yet.

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Section: Insecticidal Activitymentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

243

261

View full text Add to dashboard Cite

show abstract

“…The pesticidal activities of VIP can reach nanogram levels, which can be considered for new generation biopesticides (54). The immune inhibitor A (InhA) metalloprotease, which has similarities to the Bacillus thermoproteolyticus thermolysin, Pseudomonas aeruginosa elastase, and protease E-15 from Serratia, can specifically cleave antibacterial proteins such as cecropins and attacins produced by the insect host.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Bacillus thuringiensis at Different Growth Phases by Using an Automated Online Two-Dimensional Liquid Chromatography-Tandem Mass Spectrometry Strategy

Huang

Ding

Sun

et al. 2012

Appl Environ Microbiol

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The proteome of a new Bacillus thuringiensis subsp. kurstaki strain, 4.0718, from the middle vegetative (T 1 ), early sporulation (T 2 ), and late sporulation (T 3 ) phases was analyzed using an integrated liquid chromatography (LC)-based protein identification system. The system comprised two-dimensional (2D) LC coupled with nanoscale electrospray ionization (ESI) tandem mass spectrometry (MS/MS) on a high-resolution hybrid mass spectrometer with an automated data analysis system. After deletion of redundant proteins from the different batches and B. thuringiensis subspecies, 918, 703, and 778 proteins were identified in the respective three phases. Their molecular masses ranged from 4.6 Da to 477.4 Da, and their isoelectric points ranged from 4.01 to 11.84. Function clustering revealed that most of the proteins in the three phases were functional metabolic proteins, followed by proteins participating in cell processes. Small molecular and macromolecular metabolic proteins were further classified according to the Kyoto Encyclopedia of Genes and Genome and BioCyc metabolic pathway database. Three protoxins (Cry2Aa, Cry1Aa, and Cry1Ac) as well as a series of potential intracellular active factors were detected. Many significant proteins related to spore and crystal formation, including sporulation proteins, help proteins, chaperones, and so on, were identified. The expression patterns of two identified proteins, CotJc and glutamine synthetase, were validated by Western blot analysis, which further confirmed the MS results. This study is the first to use shotgun technology to research the proteome of B. thuringiensis. Valuable experimental data are provided regarding the methodology of analyzing the B. thuringiensis proteome (which can be used to produce insecticidal crystal proteins) and have been added to the related protein database. Bacillus thuringiensis is characterized by the production of a parasporal body during sporulation, which contains one or more Cry and/or Cyt proteins (also known as ␦-endotoxins) in crystalline form (17, 42). Many B. thuringiensis subspecies are used as bacterial insecticides and sources of genes for the recombinant bacteria and B. thuringiensis strains applied for insecticidal products (5, 31). Since the 1980s, substantial progress has been made in the development and production of new genetically engineered B. thuringiensis insecticides, especially in the transformation of insecticidal crystal proteins (ICPs), due to the ever-increasing research on the B. thuringiensis protein production mechanisms and genetic structure. For B. thuringiensis, many researchers have found great difficulty in achieving marked improvements in ICP only by traditional fermentation and mutagenesis treatment, which hinders the practical applications of B. thuringiensis. The challenge is probably rooted in the fact that except for the closely synergistic effect with spore formation (2), ICPs are synthesized via multiple intracellular reactions, which are further complicated by various factors, including c...

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“…Zhu et al (2006) have shown that B. thuringiensis YBT 1520 strain producing Cry1Aa, 1Ab, 1Ac, and Cry2 toxins after transformation with a plasmid containing the gene coding for synthesis of Vip3Aa7 had 10-fold more toxicity against S. exigua, than nontransformed parental strain. However, the transformed strain had the same level of toxicity against H. armigera as that parental YBT 1520 strain.…”

Section: Discussionmentioning

confidence: 99%

Interaction between toxin crystals and vegetative insecticidal proteins of Bacillus thuringiensis in lepidopteran larvae

2017

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Insecticides based on crystalline toxins of Bacillus thuringiensis are very good biological plant protection products. However, the spectrum of activity of some toxins is narrow or resistance among insects has been developed. We tested the insecticidal activity of crystals of the B. thuringiensis MPU B9 strain alone and supplemented with Vip3Aa proteins against important pests: Spodoptera exigua Hübner (Lepidoptera: Noctuidae), Cydia pomonella L. (Lepidoptera: Tortricidae) and Dendrolimus pini L. (Lepidoptera: Lasiocampidae). The Cry toxins were more active for D. pini but less active against S. exigua and C. pomonella than Vip3Aa. Supplementation of Cry toxins by small amounts of vegetative insecticidal proteins demonstrated synergistic effect and significantly enhanced the toxicity of the insecticide. The results indicate the utility of Cry and Vip3Aa toxins mixtures to control populations of crops and forests insect pests.

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Vegetative insecticidal protein enhancing the toxicity of Bacillus thuringiensis subsp kurstaki against Spodoptera exigua

Cited by 50 publications

References 18 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Proteomic Analysis of Bacillus thuringiensis at Different Growth Phases by Using an Automated Online Two-Dimensional Liquid Chromatography-Tandem Mass Spectrometry Strategy

Interaction between toxin crystals and vegetative insecticidal proteins of Bacillus thuringiensis in lepidopteran larvae

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