Insect resistance conferred by 283-kDa Photorhabdus luminescens protein TcdA in Arabidopsis thaliana

Dong, Liang; Burton, Stephanie; Glancy, Todd; Li, Ze-Sheng; Hampton, Ronnie E; Meade, Thomas; Merlo, Donald J.

doi:10.1038/nbt866

Cited by 100 publications

(45 citation statements)

References 20 publications

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“…[See online article for color version of this figure. ] transgenic Arabidopsis (Arabidopsis thaliana) plants (Liu et al, 2003) gave almost complete protection against larvae of the lepidopteran tobacco hornworm (Manduca sexta). Leaf extracts from these plants were also toxic to corn rootworm, showing cross-species protection.…”

Section: Photorhabdus Luminescens Insecticidal Proteinsmentioning

confidence: 99%

Biotechnological Prospects for Engineering Insect-Resistant Plants

Gatehouse

2008

Plant Physiology

194

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Insect-resistant crops have been one of the major successes of applying plant genetic engineering technology to agriculture; cotton (Gossypium hirsutum) resistant to lepidopteran larvae (caterpillars) and maize (Zea mays) resistant to both lepidopteran and coleopteran larvae (rootworms) have become widely used in global agriculture and have led to reductions in pesticide usage and lower production costs (Toenniessen et al., 2003;Brookes and Barfoot, 2005).The source of the insecticidal toxins produced in commercial transgenic plants is the soil bacterium Bacillus thuringiensis (Bt). Bt strains show differing specificities of insecticidal activity toward pests, and constitute a large reservoir of genes encoding insecticidal proteins, which are accumulated in the crystalline inclusion bodies produced by the bacterium on sporulation (Cry proteins, Cyt proteins) or expressed during bacterial growth (Vip proteins). The threedomain Cry proteins have been extensively studied; their mechanism of action involves a proteolytic activation step, which occurs in the insect gut after ingestion, followed by interaction of one or both of domains II and III with ''receptors'' on the surface of cells of the insect gut epithelium. This interaction leads to oligomerization of the protein, and domain I is then responsible for the formation of an open channel through the cell membrane . The resulting ionic leakage destroys the cell, leading to breakdown of the gut, bacterial proliferation, and insect death.However, not all pests are adequately targeted by the Bt toxins used at present, and there is still a need to develop solutions to specific problems, such as resistance to sap-sucking pests and pests of stored products. This Update will review some developments to the basic Bt strategy and selected alternative methods for engineering insect resistance.

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Section: Photorhabdus Luminescens Insecticidal Proteinsmentioning

confidence: 99%

Biotechnological Prospects for Engineering Insect-Resistant Plants

Gatehouse

2008

Plant Physiology

194

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“…are two bacterial genera belonging to the family Enterobacteriaceae, known to be associated with entomopathogenic nematodes (1-4) These bacteria represent potential sources for new genes encoding potent insecticidal toxins that could be put into plants as alternatives to Bacillus thuringiensis genes (5). Gene sequence analysis of Xenorhabdus and Photorhabdus bacteria show that these organisms contain a family of related toxin complex (tc)…”

mentioning

confidence: 99%

Insecticidal Toxin Complex Proteins from Xenorhabdus nematophilus

Sheets¹,

Hey²,

Fencil³

et al. 2011

Journal of Biological Chemistry

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Toxin complexes from Xenorhabdus and Photorhabdus spp. bacteria represent novel insecticidal proteins. We purified a native toxin complex (toxin complex 1) from Xenorhabdus nematophilus. The toxin complex is composed of three different proteins, XptA2, XptB1, and XptC1, representing products from class A, B, and C toxin complex genes, respectively. We showed that recombinant XptA2 and co-produced recombinant XptB1 and XptC1 bind together with a 4:1:1 stoichiometry. XptA2 forms a tetramer of ϳ1,120 kDa that bound to solubilized insect brush border membranes and induced pore formation in black lipid membranes. Co-expressed XptB1 and XptC1 form a tight 1:1 binary complex where XptC1 is C-terminally truncated, resulting in a 77-kDa protein. The ϳ30-kDa C-terminally cleaved portion of XptC1 apparently only loosely associates with this binary complex. XptA2 had only modest oral toxicity against lepidopteran insects but as a complex with co-produced XptB1 and XptC1 had high levels of insecticidal activity. Addition of co-expressed class B (TcdB2) and class C (TccC3) proteins from Photorhabdus luminescens to the Xenorhabdus XptA2 protein resulted in formation of a hybrid toxin complex protein with the same 4:1:1 stoichiometry as the native Xenorhabdus toxin complex 1. This hybrid toxin complex, like the native toxin complex, was highly active against insects.Xenorhabdus and Photorhabdus spp. are two bacterial genera belonging to the family Enterobacteriaceae, known to be associated with entomopathogenic nematodes (1-4) These bacteria represent potential sources for new genes encoding potent insecticidal toxins that could be put into plants as alternatives to Bacillus thuringiensis genes (5). Gene sequence analysis of Xenorhabdus and Photorhabdus bacteria show that these organisms contain a family of related toxin complex (tc) 2 genes located at different loci (6 -9). The toxin complexes are composed of three different classes of protein components, which, according to ffrench-Constant et al. (10,11), can be categorized as class A, B, and C proteins based upon sequence similarity and size. Class A proteins are very large, having a molecular mass of ϳ280 kDa. Class B proteins are ϳ170 kDa, and class C proteins are ϳ110 kDa. There are many different varieties of class A, B, and C proteins in both Gram-negative and Gram-positive bacteria (12-15).From earlier studies, it has been suggested that class A proteins harbor the cytotoxic effects of the Tc toxins, whereas class B and C proteins modulate and enhance the toxicity of class A proteins (16). However, recently, we elucidated the molecular mechanism of the Photorhabdus luminescens Tc complex, which consists of the class A protein TcdA1, the class B protein TcdB2, and the class C protein TccC3 or TccC5 (17). These studies revealed that the class C proteins harbor the biological activity. It was shown that TccC3 and TccC5 are ADP-ribosyltransferases, which target the actin cytoskeleton by modification of actin and Rho GTPases, respectively (17). Moreover, these studies su...

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“…Genetic engineering studies have used many genes to combat insect attack. Protease inhibitors (Haq et al, 2004), toxin A produced by Photorhabdus luminescens (Liu et al, 2003), bacterial cholesterol oxidase (Corbin et al, 2001) and avidin from birds are some of the examples. Limitations of these genes lie in their specificities against insects.…”

Section: Discussionmentioning

confidence: 99%

Computational and Real-Time RT-PCR Expression Analyses of Garlic Lectin Gene

Usman¹,

Rehman²,

Khan³

et al. 2015

IJAB

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Sucking insect pests inflict heavy losses to important crops. Bt gene being unable to control sucking insects, lectin seems to be a good alternative insecticidal gene. However, studies on sequence analysis, evolutionary relationship and expression patterns of garlic lectin genes remained elusive. Therefore, this study was envisaged to explore lectin gene sequence diversity in different species, and to analyze differential expression of lectin genes in garlic bulb, leaf and root tissues. Phylogenetic reconstruction did not reveal well-defined clusters indicating divergence in lectin sequences in different plant species. Multiple alignments exhibited conservation in lectin coding sequences in the middle regions. On the other hand, both the N-and Ctermini were quite divergent and size of the coding regions varied greatly in different orthologs probably due to exonization of introns. Semi-quantitative and quantitative RT-PCR exhibited elevated expression of lectin genes in garlic bulb as compared to leaf and root tissues. this study has future implications in transforming insecticidal genes in crops against sucking insects.

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Insect resistance conferred by 283-kDa Photorhabdus luminescens protein TcdA in Arabidopsis thaliana

Cited by 100 publications

References 20 publications

Biotechnological Prospects for Engineering Insect-Resistant Plants

Biotechnological Prospects for Engineering Insect-Resistant Plants

Insecticidal Toxin Complex Proteins from Xenorhabdus nematophilus

Computational and Real-Time RT-PCR Expression Analyses of Garlic Lectin Gene

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