Relevant bibliographies by topics / Insecticidal protein

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Academic literature on the topic 'Insecticidal protein'

Author: Grafiati
Published: 1 February 2023

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Journal articles on the topic "Insecticidal protein"

1

Jiang, Kun, Yan Zhang, Zhe Chen, Dalei Wu, Jun Cai, and Xiang Gao. "Structural and Functional Insights into the C-terminal Fragment of Insecticidal Vip3A Toxin of Bacillus thuringiensis." Toxins 12, no. 7 (July 5, 2020): 438. http://dx.doi.org/10.3390/toxins12070438.

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The vegetative insecticidal proteins (Vips) secreted by Bacillus thuringiensis are regarded as the new generation of insecticidal toxins because they have different insecticidal properties compared with commonly applied insecticidal crystal proteins (Cry toxins). Vip3A toxin, representing the vast majority of Vips, has been used commercially in transgenic crops and bio-insecticides. However, the lack of both structural information on Vip3A and a clear understanding of its insecticidal mechanism at the molecular level limits its further development and broader application. Here we present the first crystal structure of the C-terminal fragment of Vip3A toxin (Vip3Aa11200–789). Since all members of this insecticidal protein family are highly conserved, the structure of Vip3A provides unique insight into the general domain architecture and protein fold of the Vip3A family of insecticidal toxins. Our structural analysis reveals a four-domain organization, featuring a potential membrane insertion region, a receptor binding domain, and two potential glycan binding domains of Vip3A. In addition, cytotoxicity assays and insect bioassays show that the purified C-terminal fragment of Vip3Aa toxin alone have no insecticidal activity. Taken together, these findings provide insights into the mode of action of the Vip3A family of insecticidal toxins and will boost the development of Vip3A into more efficient bio-insecticides.
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2

Jiang, Kun, Xiaoyue Hou, Lu Han, Tongtong Tan, Zhanglei Cao, and Jun Cai. "Fibroblast Growth Factor Receptor, a Novel Receptor for Vegetative Insecticidal Protein Vip3Aa." Toxins 10, no. 12 (December 18, 2018): 546. http://dx.doi.org/10.3390/toxins10120546.

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Vegetative insecticidal proteins (Vips), which are secreted by some Bacillus thuringiensis strains during vegetative growth, exhibit high virulence to many pests. Vip3A proteins have been used commercially both in some bio-insecticides and in transgenic crops; however, compared with insecticidal crystal proteins, the mechanism of action of Vip3A is still unclear. In this work, we indicated that the fibroblast growth factor receptor-like protein (Sf-FGFR) from the membrane of Sf9 cells could bind to Vip3Aa. The interaction between Vip3Aa and Sf-FGFR was confirmed by pull-down assays and dot blotting experiment in vitro. The binding affinity between Vip3Aa and extracellular regions of Sf-FGFR (GST-FGFR-N) was determined by microscale thermophoresis assay (MST). Moreover, Vip3Aa-Flag could be co-immunoprecipitated with Sf-FGFR-V5 ex vivo. Furthermore, knockdown of Sf-FGFR gene in Sf9 cells resulted in reducing the mortality of those cells to Vip3Aa. In summary, our data indicated that Sf-FGFR is a novel receptor for Vip3Aa.
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Knox, Oliver G. G., Greg A. Constable, Bruce Pyke, and V. V. S. R. Gupta. "Environmental impact of conventional and Bt insecticidal cotton expressing one and two Cry genes in Australia." Australian Journal of Agricultural Research 57, no. 5 (2006): 501. http://dx.doi.org/10.1071/ar05366.

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Genetically modified Bt cotton, expressing the Cry1Ac protein for specific insecticidal activity against economically significant lepidopteran pests, has been available commercially in Australia since 1996. This technology has been improved and superseded by the addition of a second gene, allowing new varieties to express both the Cry1Ac the Cry2Ab proteins. Bt cotton offers several advantages to the grower, mainly through reduced insecticide spray requirements. The environmental benefits of reduced insecticide usage are assessed in this paper using the environmental impact quotient (EIQ). The assessment included consideration of the impact of the expressed transgenic proteins Cry1Ac and Cry2Ab. EIQ values of the Cry1Ac and Cry2Ab proteins were calculated at 9.9 and 7.9, respectively. Bt protein expression, plant biomass, insecticide application records, constituent of active ingredient, and insecticide EIQ values were used to produce an environmental impact (EI) value for insecticide use (kg a.i./ha) for conventional non-GM and single- and 2-gene Bt cotton for the 1997–98 to 2003–04 seasons. Inclusion of the Cry proteins in the assessment increased the EI values for Bt cotton by only 2%. The average insecticide EI value, for 2002–03 and 2003–04 seasons, for conventional cotton was 135 kg a.i./ha, whereas for the 2-gene Bt variety it was only 28 kg a.i./ha. Results of the EI evaluation indicate that, due to changes in insecticidal choice and reduction in usage, there was a reduction of >64% in EI from growing Bt cotton compared with conventional non-GM cotton in Australia.
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Shan, Yinxue, Minghui Jin, Swapan Chakrabarty, Bo Yang, Qi Li, Ying Cheng, Lei Zhang, and Yutao Xiao. "Sf-FGFR and Sf-SR-C Are Not the Receptors for Vip3Aa to Exert Insecticidal Toxicity in Spodoptera frugiperda." Insects 13, no. 6 (June 14, 2022): 547. http://dx.doi.org/10.3390/insects13060547.

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Vip3Aa is a novel insecticidal protein secreted by Bacillus thuringiensis (Bt) during its vegetative growth stages. It has high insecticidal activity against lepidopteran pests such as Spodoptera frugiperda, and has no cross-resistance with Cry insecticidal proteins. As a new type of insecticide, it plays an important role in controlling agricultural pests. However, the insecticidal mechanism of the Vip3Aa toxin, especially its definite receptors, have not been fully revealed. In this study, the previously reported Vip3Aa receptor genes Sf-FGFR and Sf-SR-C were knocked out separately using the CRISPR/Cas9 system. Bioassay results showed that the sensitivity of these two knockout strains to Vip3Aa were not significantly changed compared to that of the normal strain. The current results are not consistent with the previously reports that Sf-SR-C and Sf-FGFR were the receptors of Vip3Aa in vitro. This suggests that the Sf-SR-C and Sf-FGFR genes we tested may not be critical in the mode of action of Vip3Aa in vivo in Spodoptera frugiperda.
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5

Rajagopal, Raman, Naresh Arora, Swaminathan Sivakumar, Nagarjun G. V. Rao, Sharad A. Nimbalkar, and Raj K. Bhatnagar. "Resistance of Helicoverpa armigera to Cry1Ac toxin from Bacillus thuringiensis is due to improper processing of the protoxin." Biochemical Journal 419, no. 2 (March 27, 2009): 309–16. http://dx.doi.org/10.1042/bj20081152.

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The bacterium Bacillus thuringiensis produces ICPs (insecticidal crystal proteins) that are deposited in their spore mother cells. When susceptible lepidopteran larvae ingest these spore mother cells, the ICPs get solubilized in the alkaline gut environment. Of approx. 140 insecticidal proteins described thus far, insecticidal protein Cry1Ac has been applied extensively as the main ingredient of spray formulation as well as the principal ICP introduced into crops as transgene for agricultural crop protection. The 135 kDa Cry1Ac protein, upon ingestion by the insect, is processed successively at the N- and C-terminus by the insect midgut proteases to generate a 65 kDa bioactive core protein. The activated core protein interacts with specific receptors located at the midgut epithilium resulting in the lysis of cells and eventual death of the larvae. A laboratory-reared population of Helicoverpa armigera displayed 72-fold resistance to the B. thuringiensis insecticidal protein Cry1Ac. A careful zymogram analysis of Cry1Ac-resistant insects revealed an altered proteolytic profile. The altered protease profile resulted in improper processing of the insecticidal protein and as a consequence increased the LC50 concentrations of Cry1Ac. The 135 kDa protoxin-susceptible insect larval population processed the protein to the biologically active 65 kDa core protein, while the resistant insect larval population yielded a mixture of 95 kDa and 68 kDa Cry1Ac polypeptides. N-terminal sequencing of these 95 and 68 kDa polypeptides produced by gut juices of resistant insects revealed an intact N-terminus. Protease gene transcription profiling by semi-quantitative RT (reverse transcription)–PCR led to the identification of a down-regulated HaSP2 (H. armigera serine protease 2) in the Cry1Ac-resistant population. Protease HaSP2 was cloned, expressed and demonstrated to be responsible for proper processing of insecticidal protoxin. The larval population displaying resistance to Cry1Ac do not show an altered sensitivity against another insecticidal protein, Cry2Ab. The implications of these observations in the context of the possibility of development of resistance and its management in H. armigera to Cry1Ac through transgenic crop cultivation are discussed.
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Lu, Xingxing, Huan Xu, Xiaoming Zhang, Tengda Sun, Yufan Lin, Yongheng Zhang, Honghong Li, et al. "Design, Synthesis and Bioactivity of Novel Low Bee-Toxicity Compounds Based on Flupyrimin." Molecules 27, no. 18 (September 19, 2022): 6133. http://dx.doi.org/10.3390/molecules27186133.

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Neonicotinoids are important insecticides for controlling aphids in agriculture. Growing research suggested that neonicotinoid insecticides are a key factor causing the decline of global pollinator insects, such as bees. Flupyrimin (FLP) is a novel nicotinic insecticide with unique biological properties and no cross-resistance, and is safe for pollinators. Using FLP as the lead compound, a series of novel compounds were designed and synthesized by replacing the amide fragment with a sulfonamideone. Their structures were confirmed by 1H NMR, 13C NMR and HRMS spectra. Bioassay results showed that compound 2j had good insecticidal activity against Aphis glycines with an LC50 value of 20.93 mg/L. Meanwhile, compound 2j showed significantly lower acute oral and contact toxicity to Apis mellifera. In addition, compound 2j interacted well with the protein in insect acetylcholine binding protein (AChBP). The molecular docking on honeybee nicotinic acetylcholine receptor (nAChR) indicated that the sulfonamide group of compound 2j did not form a hydrogen bond with Arg173 of the β subunit, which conforms to the reported low bee-toxicity conformation. In general, target compound 2j can be regarded as a bee-friendly insecticide candidate.
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Ellis, R. Tracy, Brian A. Stockhoff, Lisa Stamp, H. Ernest Schnepf, George E. Schwab, Mark Knuth, Josh Russell, Guy A. Cardineau, and Kenneth E. Narva. "Novel Bacillus thuringiensis Binary Insecticidal Crystal Proteins Active on Western Corn Rootworm, Diabrotica virgifera virgifera LeConte." Applied and Environmental Microbiology 68, no. 3 (March 2002): 1137–45. http://dx.doi.org/10.1128/aem.68.3.1137-1145.2002.

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ABSTRACT A new family of insecticidal crystal proteins was discovered by screening sporulated Bacillus thuringiensis cultures for oral activity against western corn rootworm (WCR) larvae. B. thuringiensis isolates PS80JJ1, PS149B1, and PS167H2 have WCR insecticidal activity attributable to parasporal inclusion bodies containing proteins with molecular masses of ca. 14 and 44 kDa. The genes encoding these polypeptides reside in apparent operons, and the 14-kDa protein open reading frame (ORF) precedes the 44-kDa protein ORF. Mutagenesis of either gene in the apparent operons dramatically reduced insecticidal activity of the corresponding recombinant B. thuringiensis strain. Bioassays performed with separately expressed, biochemically purified 14- and 44-kDa polypeptides also demonstrated that both proteins are required for WCR mortality. Sequence comparisons with other known B. thuringiensis insecticidal proteins failed to reveal homology with previously described Cry, Cyt, or Vip proteins. However, there is evidence that the 44-kDa polypeptide and the 41.9- and 51.4-kDa binary dipteran insecticidal proteins from Bacillus sphaericus are evolutionarily related. The 14- and 44-kDa polypeptides from isolates PS80JJ1, PS149B1, and PS167H2 have been designated Cry34Aa1, Cry34Ab1, and Cry34Ac1, respectively, and the 44-kDa polypeptides from these isolates have been designated Cry35Aa1, Cry35Ab1, and Cry35Ac1, respectively.
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8

Sopko, Megan S., Kenneth E. Narva, Andrew J. Bowling, Heather E. Pence, James J. Hasler, Theodore J. Letherer, Cory M. Larsen, and Marc D. Zack. "Modification of Vip3Ab1 C-Terminus Confers Broadened Plant Protection from Lepidopteran Pests." Toxins 11, no. 6 (June 3, 2019): 316. http://dx.doi.org/10.3390/toxins11060316.

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Vegetative insecticidal proteins (Vips) from Bacillus thuringiensis (Bt) are unique from crystal (Cry) proteins found in Bt parasporal inclusions as they are secreted during the bacterial vegetative growth phase and bind unique receptors to exert their insecticidal effects. We previously demonstrated that large modifications of the Vip3 C-terminus could redirect insecticidal spectrum but results in an unstable protein with no lethal activity. In the present work, we have generated a new Vip3 protein, Vip3Ab1-740, via modest modification of the Vip3Ab1 C-terminus. Vip3Ab1-740 is readily processed by midgut fluid enzymes and has lethal activity towards Spodoptera eridania, which is not observed with the Vip3Ab1 parent protein. Importantly, Vip3Ab1-740 does retain the lethal activity of Vip3Ab1 against other important lepidopteran pests. Furthermore, transgenic plants expressing Vip3Ab1-740 are protected against S. eridania, Spodoptera frugiperda, Helicoverpa zea, and Pseudoplusia includens. Thus, these studies demonstrate successful engineering of Vip3 proteins at the C-terminus to broaden insecticidal spectrum, which can be employed for functional expression in planta.
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López-Pazos, S. A., F. M. Chavarrio Cañas, and A. C. Rojas Arias. "Insecticidal and Potato Growth Stimulation Activity of Bacillus thuringiensis kurstaki HD-1." Mikrobiolohichnyi Zhurnal 84, no. 4 (January 17, 2023): 9–29. http://dx.doi.org/10.15407/microbiolj84.04.009.

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Bacillus thuringiensis (Bt) produces Cry toxins against pest insects. Cry proteins are conformed by domains related to pore formation and recognition of protein receptors. Plant-induced systemic resistance (ISR) is triggered due to pest attack, it could be activated by Bacillus sp. Tecia solanivora (Ts) is a potato pest, susceptible to Cry1Ac and Cry1B proteins. This paper indicates the endorsement of Bt kurstaki HD-1 (BtkHD1) in relation to Ts control (Cry1Ac and Cry1B proteins), potato growth promotion, and plant ISR due to pests related to the BtkHD1-potato system. To ensure that ongoing quality control of BtkHD1 was maintained, crystal synthesis (microscopy), cry1 genes presence, and Cry protein production were checked. Bioassays Ts larvae and potato plantlets and an in silico analysis of the hybrid Cry1Ac-Cry1Ba protein and potato ISR related to the BtkHD1 infl uence were performed. Bioassay on Ts larvae shows an LC50 of 536 ng/cm2 of diet. A potato growth promotion assay revealed the effect of BtkHD1 on the length and dry weight of stems. The prospective analysis took into account relevant factors affecting the biological function of the hybrid protein focused on domain II. In silico identification of 15 BtkHD1 proteins and 68 potato proteins related to plant ISR due to pests was completed. This project serves to validation of toxicity on Ts larvae and potato growth effect based on BtkHD1, including a forward analysis of the hybrid Cry1Ac1-Cry1Ba1, and proteins associated with this strain and potato for eliciting plant ISR due to pests.
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Edrington, Thomas, Rong Wang, Lucas McKinnon, Colton Kessenich, Kimberly Hodge-Bell, Wenze Li, Jianguo Tan, et al. "Food and feed safety of the Bacillus thuringiensis derived protein Vpb4Da2, a novel protein for control of western corn rootworm." PLOS ONE 17, no. 8 (August 3, 2022): e0272311. http://dx.doi.org/10.1371/journal.pone.0272311.

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Western corn rootworm (WCR), Diabrotica virgifera virgifera, LeConte, is an insect pest that poses a significant threat to the productivity of modern agriculture, causing significant economic and crop losses. The development of genetically modified (GM) crops expressing one or more proteins that confer tolerance to specific insect pests, such as WCR, was a historic breakthrough in agricultural biotechnology and continues to serve as an invaluable tool in pest management. Despite this, evolving resistance to existing insect control proteins expressed in current generation GM crops requires continued identification of new proteins with distinct modes of action while retaining targeted insecticidal efficacy. GM crops expressing insecticidal proteins must undergo extensive safety assessments prior to commercialization to ensure that they pose no increased risk to the health of humans or other animals relative to their non-GM conventional counterparts. As part of these safety evaluations, a weight of evidence approach is utilized to assess the safety of the expressed insecticidal proteins to evaluate any potential risk in the context of dietary exposure. This study describes the food and feed safety assessment of Vpb4Da2, a new Bacillus thuringiensis insecticidal protein that confers in planta tolerance to WCR. Vpb4Da2 exhibits structural and functional similarities to other insect control proteins expressed in commercialized GM crops. In addition, the lack of homology to known toxins or allergens, a lack of acute toxicity in mice, inactivation by conditions commonly experienced in the human gut or during cooking/food processing, and the extremely low expected dietary exposure to Vpb4Da2 provide a substantial weight of evidence to demonstrate that the Vpb4Da2 protein poses no indication of a risk to the health of humans or other animals.
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Dissertations / Theses on the topic "Insecticidal protein"

1

Choma, Christin Teresa. "Structural characterization of the insecticidal protein from Bacillus thuringiensis." Thesis, University of Ottawa (Canada), 1990. http://hdl.handle.net/10393/5624.

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During sporulation, Baccilus thuringiensis subsp. kurstaki produces a crystalline inclusion body which is toxic upon ingestion by susceptible Lepidopteran larvae. The major component of crystals from Lepidopteran-specific subspecies of B. thuringiensis is a 130-kDa protein, protoxin. Following ingestion by susceptible larvae, protoxin is proteolyzed to yield a 58-70 kDa toxic fragment, toxin. In the present study, a simplified procedure was used for isolating and purifying toxin generated by the tryptic digestion of protoxin from B. thuringiensis subsp. kurstaki HD-73. Characterization of this toxin showed that it is derived from the N-terminal half of the protoxin molecule. The toxin is insoluble at neutral pH values but is moderately soluble at alkaline values above pH 9. Application of several spectroscopic and theoretical procedures to the purified toxin showed that the protein is composed of approximately equal amounts of a $\alpha$-helix, $\beta$-sheet and random coil structures. The tertiary structure of toxin was shown to be comprised of two primary domains; these domains correspond to the toxic and specificity (or binding) domains predicted from analysis of protoxin gene nucleotide sequences. Evidence was obtained that at least one additional domain is present as a structural component of the C-terminal specificity domain. Both the toxic moiety within the protoxin molecule and free toxin were found to be unusually resistant to unfolding by chemical denaturants and to proteolysis. In contrast, the C-terminal half of protoxin could be readily unfolded and was extremely susceptible to proteolytic digestion. The unfolded protoxin and unfolded toxin were shown to refold rapidly into their native and biologically active conformations. Evidence was obtained that the conformation of the toxic moiety of protoxin is very similar to the conformation of toxin. Chemical modification of the cysteine and lysine residues in the protoxin did not affect the biological activity of the protein. However, the introduction of positive, negative or neutral groups onto these residues had a large effect on the solubility of the protein. These results, along with the results obtained from the unfolding/folding, studies, strongly indicate that the primary function of the C-terminal half of the protoxin molecule is to promote the formation of a stable crystal.
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2

Bietlot, Henri P. "Characterization of the insecticidal crystal protein from Bacillus thuringiensis." Thesis, University of Ottawa (Canada), 1990. http://hdl.handle.net/10393/5668.

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Bacillus thuringiensis produces a crystalline inclusion body composed of a 130-kDa protein which is rendered toxic upon ingestion by lepidoteran larvae. It was shown that proteinases adsorb on the surface of the crystalline body lead to proteolysis of the protein crystal especially on solubilization in alkali. Extensive washing of the protein crystal was shown to remove these proteinases and give a stable preparation. Exposure of the protein crystal to simulated sunlight results in a loss of toxicity and in the destruction of the side-chains of tryptophan, histidine, tyrosine and methionine. Destruction of amino acid side-chains is not the primary cause of the photo-inactivation of the protein crystal. The finding that all the disulfide linkages in the protein crystal are interchain and symmetrical accounts for its alkaline lability and for the high degree of conservation in the primary structure of the cystine-containing regions of the protein from various subspecies. (Abstract shortened by UMI.)
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3

Ahmad, Wasim. "Genetics and biochemistry of Bacillus thuringiensis insecticidal protein [?]-endotoxin." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.306309.

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4

Bietlot, Henri P. "Characterization of the insecticidal protein from Bacillus thuringiensis: The importance of DNA-protein interactions." Thesis, University of Ottawa (Canada), 1993. http://hdl.handle.net/10393/6598.

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Many strains of Bacillus thuringiensis produce a crystalline inclusion during sporulation which is toxic to insect larvae. The major component of crystals toxic to lepidopteran larvae is a 130-kDa protein, the protoxin. Following ingestion by susceptible insect larvae, protoxin is proteolysed by larval gut proteinases to yield a 58-70 kDa toxic fragment, toxin. A procedure was developed to prepare purified toxin for chemical characterization. Toxin generated by bovine trypsin was shown to be composed of the amino acid residues that span position 29-623 of the protoxin. The results obtained from competitive labelling experiments on the protoxin show that the functional groups of the lysine and tyrosine residues do not exhibit regular titration behaviour over the pH range of 7 to 10. These results indicate that the majority of these groups are not free in solution but are involved in inter and intra molecular interactions. During purification by ion exchange chromatography of the bovine generated toxin, it was discovered that the toxin could be separated into two components. One component (T2) was DNA-associated toxin, and the other was the DNA-free toxin (T1). Only one major protoxin component was observed, and it was found to be associated with DNA. The DNA from the T2 toxin varied in size from 100 to 300 base pairs, whereas the crystal and the solubilized protoxin contain 20-kilobase DNA as the major DNA component. DNase treatment converted the T2 toxin to the DNA-free T1 toxin. In contrast, the DNA in the crystal and the solubilized protoxin was resistant to DNase digestion and was not dissociated from the protein by 1.5 M NaCl. The protoxin and DNA appeared to elute as a complex with a molecular mass of greater than $2\times 10\sp6$ Da on gel-filtration chromatography. No toxin was generated from the protoxin with trypsin after extensive digestion of the protoxin with DNase or dissociation of the DNA by succinylation of the lysine residues. It is proposed that DNA binds to the carboxyl terminal half of the crystal protein and is essential for maintaining the conformational integrity required for crystal formation and generation of toxin.
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5

Yamagiwa, Masashi. "THE MODE OF ACTION OF INSECTICIDAL PROTEIN PRODUCED BY BACILLUS THURINGIENSIS." Kyoto University, 2000. http://hdl.handle.net/2433/181060.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第8437号
農博第1121号
新制||農||801(附属図書館)
学位論文||H12||N3394(農学部図書室)
UT51-2000-F341
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 天知 輝夫, 教授 桒原 保正, 教授 加藤 暢夫
学位規則第4条第1項該当
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Truong, Hung Phuc. "Fate of Cry Toxins from Bacillus thuringiensis in soil." Thesis, Montpellier, 2015. http://www.theses.fr/2015MONTS210.

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Les propriétés insecticides du Bacillus thuringiensis, découvert par ShigentaneIshiwatari, ont été utilisées pendant des décennies comme biopesticides et cette utilisation a augmenté rapidement en raison de préoccupations au sujet des effets environnementaux négatifs des pesticides chimiques. Actuellement, la toxine Bt dans la forme de biopesticides et des plantes transgéniques Bt peut compléter ou remplacer les pesticides chimiques. Il y a peu d’indication que la toxine Bt a un effet nocif pour l'environnement ou la santé humaine. Néanmoins, il ya des préoccupations que les cultures transgéniques commerciales peuvent avoir des effets néfastes sur l'environnement. Après son introduction dans le sol l'exsudation racinaire et la dégradation des résidus végétaux, la toxine Bt interagit avec les particules de sol. Les interactions de la toxine Bt avec des particules de sol influencent sa mobilité, sa biodisponibilité, sa persistance et sa toxicité.Dans cette étude, nous visons à établir l'importance relative des facteurs biologiques et physico-chimiques dans la détermination de la dynamique des protéines Cry détectables dans les sols, de clarifier si la protéine adsorbée conserve ses propriétés insecticides et d'identifier les propriétés du sol qui déterminent le devenir des protéines Cry dans le sol. Les résultats montrent que les protéines Cry ont une forte affinité sur la surface du sol. Cependant, il y avait peu de relation entre l'affinité pour le sol ou le rendement d'extraction et les propriétés du sol, y compris la teneur en argile, teneur en carbone organique et le pH du sol. Il y avait peu de rapport entre l'affinité et le rendement d'extraction. Les protéines diffèrent à la fois dans leur affinité pour les sols et leurs rendements d'extraction.Une évaluation du rôle du sol et des facteurs environnementaux dans le sort des protéines Cry de la formulation de biopesticides commerciale a montré un déclin rapide de la protéine Cry détectable soumise aux rayons du soleil sous la condition de laboratoire, alors que peu d'effet a été observé dans des conditions de terrain. La demi-vie des protéines dans le sol dans des conditions naturelles était d'environ 1 semaine. Des effets de la température forts ont été observés, mais ils diffèrent pour les biopesticides et la protéine purifiée, indiquant différentes étapes limitantes. Pour le biopesticide, la baisse observée était ralenties par des facteurs biologiques, y compris éventuellement sporulation. En revanche pour des protéines purifiées, augmentation de la température améliorée des changements conformationnels de la protéine adsorbée du sol, conduisant à une fixation et, par conséquent diminué efficacité d'extraction qui a diminué avec le temps. En outre, l'étude de la persistance de diverses protéines Cry dans les sols contrastés a été réalisée par immuno-détection et dosage biologique a montré que la toxine extractible diminue avec incubation allant jusqu'à quatre semaines. L'activité insecticide était toujours maintenue à l'état adsorbé, mais a disparue après deux semaines d'incubation à 25°C. La baisse de la protéine extractible et la toxicité était beaucoup plus faible à 4°C à 25°C. La stérilisation du sol n'a pas eu d'effet significatif sur la persistance de la toxine Cry indiquant que le déclin observé était provoqué par la fixation en fonction du temps de la protéine adsorbée ce qui diminue la quantité de toxine Cry extractable, la dégradation de la protéine par l’activité microbienne jouant un rôle plus mineur.L’exposition des insectes aux protéines Cry sous la forme adsorbé pourrait avoir un impact significatif sur les insectes cibles et même les insectes non cibles, et devrait être plus étudiée afin de déterminer son impact potentiel
The insecticidal properties of Bacillus thuringiensis, discovered by Shigentane Ishiwatari, have been used for decades as biopesticides and this use has been increasing rapidly because of concerns about the negative environmental effects of chemical pesticides. Currently, Bt toxin in the form of both biopesticides and Bt transgenic plantsmay supplement or replace chemical pesticide. There is little evidence to demonstrate that Bt toxin has any harmful effect to the environment or to human health. Nevertheless, there are concerns that commercial transgenic crops may have harmful impacts on the environment. After release into soil via root exudation and breakdown of plant residues, Bt toxin interacts with soil particles. The interactions of Bt toxin with soil particles influence its mobility, its bioavailability, its persistence and its toxicity. In this study, we aim to establish the relative importance of biological and physicochemical factors in the determination of the dynamics of detectable Cry proteins in soils, to clarify if adsorbed protein maintains its insecticidal properties and to identify the soil properties that determine the fate of Cry proteins in soil. The results show that Cry proteins have strong affinity on soil surface. However, there was little relationship between affinity for soil or the extraction yield and soil properties including clay content, organic carbon content and soil pH. There was little relationship between the affinity and the extraction yield. The proteins differ in both their affinity for soil and their extraction yields.An assessment of role of soil and environmental factors in the fate of Cry protein from commercial biopesticide formulation showed a rapid decline of detectable Cry protein subjected to direct sunlight under the laboratory condition, whereas, little effect was observed under field conditions. The half-life of proteins in soil under natural conditions was about one week. Strong temperature effects were observed, but theydiffered for biopesticide and purified protein, indicating different limiting steps. For biopesticide, the observed decline was due to biological factors, possibly including sporulation. In contrast for purified proteins, increased temperature enhanced conformationalchanges of the soil-adsorbed protein, leading to fixation and hence extraction efficiency decreased that decreased with time. Moreover, the study of persistence of various Cry proteins in contrasting soils was carried out by immuno-detection and bioassay showed that extractable toxin decreased with incubation of up to four weeks. Insecticidal activity was still retained in the adsorbed state, but lost after two weeks of incubation at 25°C. The decline in extractable protein and toxicity was much lower at 4°C than 25°C. There was no significant effect of soil sterilization to persistence of Cry toxin indicating that decrease in detectable Cry toxin in soil may be time-dependent fixation of adsorbed protein as well as decreasing solubilization in larva midgut, but not microbial breakdown.Exposition to Cry in the adsorbed form could have a significant impact on target and even non target insects and should be investigation to determine the potential impact
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Liu, Yilin. "Investigating insect molecular responses to two plant defense proteins and characterizing a novel insecticidal protein from Arabidopsis." Texas A&M University, 2005. http://hdl.handle.net/1969.1/4855.

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The molecular interaction between plants and insects is dynamic and multifaceted. We are interested in understanding the molecular mechanism that insects utilize to overcome plant defense proteins, as well as discovering novel plant insecticidal proteins. Three projects were developed. First, we evaluated the effects of soybean cysteine protease inhibitor (soyacystatin N, scN) on the growth and development in southern corn rootworm. Both subtractive suppressed hybridization (SSH) and cDNA microarray analyses were used to uncover the changes of gene expression profiles in southern corn rootworm under the scN challenge. The counterdefense-related genes were identified, suggesting that southern corn rootworm deployed several regulatory mechanisms to overcome the dietary scN. Second, to identify and confirm insecticidal properties of vegetative storage protein 2 in Arabidopsis (AtVSP2), the gene was cloned and expressed in E.coli. This protein showed acid phosphatase activity. Feeding assay indicated that AtVSP increased the mortality and delayed the development of two coleopteran and one dipteran insects. Third, to identify the molecular mechanism of this novel insecticidal protein, P element mutagenesis was utilized to generate AtVSP resistant mutants (VRs). Two balanced VR mutants and their revertants were generated, and can be used to further characterize the genetic loci of P element inserted in the mutants.
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Clairmont, François. "Structure of the insecticidal crystal protein from Bacillus thuringiensis var. kurstaki HD-73." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0015/NQ48094.pdf.

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Audtho, Mongkon. "Mode of action of Cry2Aa, a Bacillus thuringiensis dual active insecticidal crystal protein /." The Ohio State University, 2001. http://rave.ohiolink.edu/etdc/view?acc_num=osu1486397841221052.

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Wilson, F. Douglas, and Hollis M. Flint. "Field Performance of Cotton Genetically Modified to Express Insecticidal Protein from Bacillus thuringiensis." College of Agriculture, University of Arizona (Tucson, AZ), 1991. http://hdl.handle.net/10150/208376.

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Five transgenic lines of cotton, Gossypium hirsutum L., carrying the delta-endotoxin gene from Bacillus thuringiensis Berl., and two control cultivars, Coker 312 (the parent stock) and MDS1N (an adapted nectoriless line) were evaluated at the Maricopa Agricultural Centerfor resistance to attack by several insect pests and for agronomic properties. The transgenic lines were highly resistant to pink bollworm (PBW), Pectinophora gossypiella (Saunders), as shown by 90% fewer rosetted blooms, 96% fewer PBW recovered from incubated bolls, and 92% less seed damage than in the control cultivars. The transgenic lines were highly resistant to saltmarsh caterpillar, Estigmene acres (Drury), and beet annyworm, Spodoptera exigua (Hbn.), as shown by minimal damage to transgenic leaves and almost complete defoliation of control leaves. The transgenic lines were virtually immune to cotton leafperforator, Bucculatrix thurberiella Busch as shown by no apparent damage to transgenic leaves, and many mines, "horseshoes", and feeding areas on the control leaves. Compared to Coker 312, one transgenic line yielded more lint, and one yielded less. Four transgenic lines had higher lint percentages and all five had smaller bolls and were later maturing than Coker 312. Compared to MD51N, no transgenic line yielded more lint and one yielded less. All five transgenic lines had lower lint percentages, three had smaller bolls, and three were earlier maturing than MDS1N (USDA, ARS, Western Cotton Research Laboratory in cooperation with Monsanto Co. and Arizona Agricultural Experiment Station).
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Books on the topic "Insecticidal protein"

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Temeyer, Kevin Bruce. Monoclonal antibodies to crystal protein of Bacillus thuringiensis subspecies Israelensis. [Washington, D.C.?: U.S. Dept. of Agriculture?], 1987.

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Macoun, W. T. How to protect fruits, vegetables and ornamental plants from insects and fungous diseases. [Ottawa?: s.n., 1997.

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Gill, Sarjeet S., and Tarlochan S. Dhadialla. Insect Midgut and Insecticidal Proteins. Elsevier Science & Technology Books, 2014.

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Insect Midgut and Insecticidal Proteins. Elsevier, 2014. http://dx.doi.org/10.1016/c2013-0-12819-x.

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Gill, Sarjeet S., and Tarlochan S. Dhadialla. Insect Midgut and Insecticidal Proteins. Elsevier Science & Technology Books, 2014.

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McBurney, John W. Pesticides and Neurodegenerative Disorders. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190490911.003.0008.

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Neurodegenerative diseases, which are characterized by neuronal degeneration, include Alzheimer disease (AD), Parkinson disease (PD), and amyotrophic lateral sclerosis (ALS). Their worldwide prevalence is increasing as the global population ages. The causes reflect interactions between genetics and environmental factors such as increasing urbanization, industrialization, and widespread use of chemicals, including insecticides, fungicides, and herbicides. Epidemiologic data suggest that exposure to many of these pesticides increases the risk of neurodegeneration. The best-defined mechanism for this association is mitochondrial toxicity resulting in increased reactive oxygen species. In PD and AD, the associated accumulation of aggregates of insoluble, misfolded proteins results in the formation of Lewy bodies and neurofibrillary tangles, respectively. Pesticide exposures can be reduced by modifying food choices and applying integrated pest management in schools, businesses, and homes. Medical professionals can counsel patients about limiting exposure to pesticides and decreasing the risk of neurodegenerative disorders.
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Book chapters on the topic "Insecticidal protein"

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Li, Jade. "Insecticidal δ-Endotoxins from Bacillus Thuringiensis." In Protein Toxin Structure, 49–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22352-9_4.

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Schnepf, H. Ernest. "Bacillus thuringiensis Recombinant Insecticidal Protein Production." In Bacillus thuringiensis Biotechnology, 259–81. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-3021-2_14.

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Senthilkumar, M., N. Amaresan, and A. Sankaranarayanan. "Detection of Vegetative Insecticidal Protein (Vip) in Bacillus." In Springer Protocols Handbooks, 249–51. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-1080-0_71.

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Cordero, Mireya, M. Anwar Hossain, Nayely Espinoza, Veronica Obregon, Mariel Roman, Samantha Navarro, Laura Lina, Gerardo Corzo, and Elba Villegas. "Identifying Insect Protein Receptors Using an Insecticidal Spider Toxin." In Spider Venoms, 405–18. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-007-6389-0_22.

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Cordero, Mireya, M. Anwar Hossain, Nayely Espinoza, Veronica Obregon, Mariel Roman, Samantha Navarro, Laura Lina, Gerardo Corzo, and Elba Villegas. "Identifying Insect Protein Receptors Using an Insecticidal Spider Toxin." In Spider Venoms, 1–11. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-007-6646-4_22-1.

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Gawron-Burke, Cynthia, and James A. Baum. "Genetic Manipulation of Bacillus Thuringiensis Insecticidal Crystal Protein Genes in Bacteria." In Genetic Engineering, 237–63. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3760-1_11.

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Clark, J. Marshall. "Action of Pyrethroids on Ca2+-Stimulated ATP Hydrolyzing Activities: Protein Phosphorylation-Dephosphorylation Events in Insect Brain Fractions." In Membrane Receptors and Enzymes as Targets of Insecticidal Action, 189–211. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5113-9_10.

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Martens, J. W. M., M. Knoester, F. Weyts, A. J. A. Groffen, H. J. Bosch, B. Visser, and J. M. Vlak. "Insecticidal Activity of Autographa Californica Nuclear Polyhedroses Virus Expressing Different Bacillus Thuringiensis Crystal Protein Constructs." In Plant Production on the Threshold of a New Century, 413. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-1158-4_50.

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Milne, R., A. Z. Ge, D. Rivers, and D. H. Dean. "Specificity of Insecticidal Crystal Proteins." In ACS Symposium Series, 22–35. Washington, DC: American Chemical Society, 1990. http://dx.doi.org/10.1021/bk-1990-0432.ch004.

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Vargas, Lúcia Rosane Bertholdo, and Célia Regina Carlini. "Insecticidal and Antifungal Activities of Ribosome-inactivating Proteins." In Ribosome-inactivating Proteins, 212–22. Oxford: John Wiley & Sons, Ltd., 2014. http://dx.doi.org/10.1002/9781118847237.ch14.

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Conference papers on the topic "Insecticidal protein"

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Peng, Rong. "The structure, transcriptional regulation, and function ofHelicoverpa armigerasterol carrier protein-2, an important insecticidal target from the cotton bollworm." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.113425.

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Kryzhko, A. V., L. N. Kuznetsova, and A. V. Shirma. "Promising entomopathogenic strain of Bacillus thuringiensis 0428 effective against the Colorado beetle." In РАЦИОНАЛЬНОЕ ИСПОЛЬЗОВАНИЕ ПРИРОДНЫХ РЕСУРСОВ В АГРОЦЕНОЗАХ. Federal State Budget Scientific Institution “Research Institute of Agriculture of Crimea”, 2020. http://dx.doi.org/10.33952/2542-0720-15.05.2020.14.

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Most of the world produced biopesticides are made by entomopathogenic bacteria B. thuringiensis. So, searching for new strains of it is always necessary. In 2006, the strain B. thuringiensis 0428 was isolated from the caterpillar of the ringed silkworm. The strain 0428 is entomopathogenic against Colorado beetle larvae. The effectiveness of the strain for 5 days was 100%. On beef-extract agar this Gram-positive bacterium formed round or irregular colonies with an average diameter of 6-10 mm. The relief of the colonies is flat; the surface is matte. Colonies of B. thuringiensis 0428 are fast-growing, appearing on the surface of the beef-extract agar on the second or third day at 26-30ºC. The average cell size is 6.48±0.16 (large diameter) and 2.62±0.06 (small diameter) microns. The study of the physiological and biochemical properties of the isolated strain shown that B. thuringiensis 0428 is able to form acetyl-methyl-carbinol and lecithinase. B. thuringiensis 0428 is not able to form ureases or pigments, as well as to use citrates and galactose. But it is able to use sucrose, glucose, mannose, and salicin as a source of carbon. The strain 0428 has proteolytic activity. The strain is capable of synthesizing an insecticidal crystalline protein Cry1A and β-exotoxin. All these characteristics allow us to identify the isolated entomopathogenic strain 0428 as B. thuringiensis var. thuringiensis.
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Stranishevskaya, E. P., E. A. Matveikina, N. I. Shadura, and Y. A. Volkov. "EFFECTIVENESS OF THE INSECTICIDE AVANT, CE (CONCENTRATED EMULSION) IN THE PEST CONTROL OF EUROPEAN GRAPE MOTH ON VINEYARDS OF THE REPUBLIC OF CRIMEA." In STATE AND DEVELOPMENT PROSPECTS OF AGRIBUSINESS. DSTU-PRINT, 2020. http://dx.doi.org/10.23947/interagro.2020.1.279-282.

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The article presents data of the use of the insecticide Avant, CE (150 g / l indoxacarb) in the standard rate of consumption 0.25 and 0.30 l / ha, for protecting of vineyards from Europen grape moth with average and high population density of the pest. Usage of this preparation allowed to protect the vineyards reliably and obtain a significantly higher crop yields rather than in the control. The biological effectiveness of the insecticide Avant, CE was high during the entire period of protective measures and amounted to 78.4-82.4% in the rate of application 0.25 l / ha, and 85.8-88.7% in rate of application 0.3 l / ha.
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Li, Ting. "The GPCR/G-protein/Adenylyl Cyclase/Protein Kinase A pathway in insecticide resistance of the mosquito, Culex quinquefasciatus." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.115399.

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Boeckman, Chad. "Use of species sensitivity distributions in the characterization of risk of novel insecticidal proteins to non-target organisms." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.107854.

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Кроитору, Никита, and Сергей Пануца. "Некоторые особенности борьбы с вредителями сои в условиях Республики Молдова." In International symposium ”Actual problems of zoology and parasitology: achievements and prospects” dedicated to the 100th anniversary from the birth of academician Alexei Spassky. Institute of Zoology, Republic of Moldova, 2018. http://dx.doi.org/10.53937/9789975665902.84.

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In Moldova, 25-30% of leguminous crops are lost every year due to damage to pests and infection by toxin-forming organisms. Over 50 species of pests have been registered on soybeans, damaging the plant in different phases of development. In 2014, soybean identified 14 species of pests from which only a population of nodule weevils, soybean moth and bean firings have surpassed the economic threshold of damage. A significant positive role in reducing the number of pests is played by natural populations of parasitic and predatory entomophages. The most effective is the insecticide Proteus OD 110 with a rate of 0.75 l / ha, which protects soybean plants by 99.38-78.06% for 7-10 days.
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"Development of a biosensor for rapid detection of insecticide based on insect-derived chemosensory proteins and graphene nanocellulose paper." In 2016 ASABE International Meeting. American Society of Agricultural and Biological Engineers, 2016. http://dx.doi.org/10.13031/aim.20162460030.

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PIMOKHOVA, Lyudmila, German YaGOVENKO, Zhanna TSARAPNEVA, and Nina Kharaborkina. "Impact of efficient protective chemicals on seeds yield of white lupin." In Multifunctional adaptive feed production 27 (75). ru: Federal Williams Research Center of Forage Production and Agroecology, 2022. http://dx.doi.org/10.33814/mak-2022-27-75-65-72.

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The white lupin is a source for qualitative plant protein to provide balanced nutrition for animals and poultry. Seed and green mass yield of modern lupin varieties can be 3–5 t/ha and 70–120 t/ha respectively. In spite of valuable qualities the production crop use is insufficient. One of the reasons is infection by diseases and pests. Anthracnose is the main dangerous and harmfulness disease. As a result lupin is in dire need for high effective protective chemicals. High effectiveness (97–96%) of seed dressers Vitaros – 2.0 l/t, Maxim XL – 2.0 l/t, Divident Star – 0.5 l/t, Selest Top – 0.7 l/t, Inshurperform – 0.7 l/t was revealed against seeds’ infection with anthracnose and other diseases under field conditions. The fungicides Amistar Extra – 0.5 l/ha, Spirit – 0.7 l/ha, Rakurs – 0.4 l/ha, Kolosal Pro – 0.4 l/ha, Bamper Super – 1.5 l/ha and Zantara – 1.5 l/ha are of high effectiveness (88–93%) for protection of lupin crops. The insecticides Tabu – 0.4 l/t and Selest Top – 07 l/t were high effective (76.2–96.0%) against seedlings pests. The most effective dressers (91–96%) against aphids and weevils were the chemicals BI-58 New – 0.7 l/ha and Borey Neo – 0.2 l/ha. The use of the mentioned chemicals for white lupin protection allows manage development and harmfulness level of harmful organisms in crops and prevent significant grain yield losses.
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Reports on the topic "Insecticidal protein"

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Dillman, Adler, and Dana Ment. Novel nematode-derived insecticidal proteins for pest control. United States Department of Agriculture, January 2018. http://dx.doi.org/10.32747/2018.7604938.bard.

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Gassmann, Aaron J., and Ryan Keweshan. Durability of Corn Expressing Bacillus thuringiensis Insecticidal Proteins in Single and Stacked Events. Ames: Iowa State University, Digital Repository, 2010. http://dx.doi.org/10.31274/farmprogressreports-180814-217.

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Fridman, Eyal, and Eran Pichersky. Tomato Natural Insecticides: Elucidation of the Complex Pathway of Methylketone Biosynthesis. United States Department of Agriculture, December 2009. http://dx.doi.org/10.32747/2009.7696543.bard.

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Plant species synthesize a multitude of specialized compounds 10 help ward off pests. and these in turn may well serve as an alternative to synthetic pesticides to reduce environmental damage and health risks to humans. The general goal of this research was to perform a genetic and biochemical dissection of the natural-insecticides methylketone pathway that is specific to the glandular trichomes of the wild species of tomato, Solanumhabrochaites f. glabratum (accession PI126449). Previous study conducted by us have demonstrated that these compounds are synthesized de novo as a derivate pathway of the fatty acid biosynthesis, and that a key enzyme. designated MethylketoneSynthase 1 (MKS 1). catalyzes conversion of the intermediate B-ketoacyl- ACPs to the corresponding Cn-1 methylketones. The approach taken in this proposed project was to use an interspecific F2 population. derived from the cross between the cultivated lV182 and the wild species PIl26449. for three objectives: (i) Analyze the association between allelic status of candidate genes from the fatty acid biosynthesis pathway with the methylketone content in the leaves (ii) Perform bulk segregant analysis of genetic markers along the tomato genome for identifying genomic regions that harbor QTLs for 2TD content (iii) Apply differential gene expression analysis using the isolated glands of bulk segregant for identifying new genes that are involved in the pathway. The genetic mapping in the interspecific F2 population included app. 60 genetic markers, including the candidate genes from the FAS pathway and SSR markers spread evenly across the genome. This initial; screening identified 5 loci associated with MK content including the candidate genes MKS1, ACC and MaCoA:ACP trans. Interesting observation in this genetic analysis was the connection between shape and content of the glands, i.e. the globularity of the four cells, typical to the wild species. was associated with increased MK in the segregating population. In the next step of the research transcriptomic analysis of trichomes from high- and 10w-MK plants was conducted. This analysis identified a new gene, Methy1ketone synthase 2 (MKS2), whose protein product share sequence similarity to the thioesterase super family of hot-dog enzymes. Genetic analysis in the segregating population confirmed its association with MK content, as well as its overexpression in E. coli that led to formation of MK in the media. There are several conclusions drawn from this research project: (i) the genetic control of MK accumulation in the trichomes is composed of biochemical components in the FAS pathway and its vicinity (MKS 1 and MKS2). as well as genetic factors that mediate the morphology of these specialized cells. (ii) the biochemical pathway is now realized different from what was hypothesized before with MKS2 working upstream to I\1KS 1 and serves as the interface between primary (fatty acids) and secondary (MK) metabolism. We are currently testing the possible physical interactions between these two proteins in vitro after the genetic analysis showed clear epistatic interactions. (iii) the regulation of the pathway that lead to specialized metabolism in the wild species is largely mediated by transcription and one of the achievements of this project is that we were able to isolate and verify the specificity of the MKS1 promoter to the trichomes which allows manipulation of the pathways in these cells (currently in progress). The scientific implications of this research project is the advancement in our knowledge of hitherto unknown biochemical pathway in plants and new leads for studying a new family in plants (hot dog thioesterase). The agricultural and biotechnological implication are : (i) generation of new genetic markers that could assist in importing this pathway to cultivated tomato hence enhancing its natural resistance to insecticides, (ii) the discovery of MKS2 adds a new gene for genetic engineering of plants for making new fatty acid derived compounds. This could be assisted with the use of the isolated and verified MKS1 promoter. The results of this research were summarized to a manuscript that was published in Plant Physiology (cover paper). to a chapter in a proceeding book. and one patent was submitted in the US.
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Ullman, Diane, James Moyer, Benjamin Raccah, Abed Gera, Meir Klein, and Jacob Cohen. Tospoviruses Infecting Bulb Crops: Evolution, Diversity, Vector Specificity and Control. United States Department of Agriculture, September 2002. http://dx.doi.org/10.32747/2002.7695847.bard.

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Objectives. The overall goal of the proposed research was to develop a mechanistic understanding of tospovirus evolution, diversity and vector specificity that could be applied to development of novel methods for limiting virus establishment and spread. Our specific objectives were: 1) To characterize newly intercepted tospoviruses in onion, Hippeastrum and other bulb crops and compare them with the known tomato spotted wilt virus (TSWV) and its isolates; 2) To characterize intra- and interspecific variation in the virus transmission by thrips of the new and distinct tospoviruses. and, 3) To determine the basis of vector specificity using biological, cellular and molecular approaches. Background. New tospoviruses infecting bulb crops were detected in Israel and the US in the mid-90s. Their plant host ranges and relationships with thrips vectors showed they differed from the type member of the Tospovirus genus, tomato spotted wilt virus (TSWV). Outbreaks of these new viruses caused serious crop losses in both countries, and in agricultural and ornamental crops elsewhere. In the realm of plant infecting viruses, the tospoviruses (genus: Tospovirus , family: Bunyaviridae ) are among the most aggressive emerging viruses. Tospoviruses are transmitted by several species of thrips in a persistent, propagative fashion and the relationships between the viruses and their thrips vectors are often specific. With the emergence of new tospoviruses, new thrips vector/tospovirus relationships have also arisen and vector specificities have changed. There is known specificity between thrips vector species and particular tospoviruses, although the cellular and molecular bases for this specificity have been elusive. Major conclusions, solutions and achievements. We demonstrated that a new tospovirus, iris yellow spot virus (IYSV) caused "straw bleaching" in onion (Allium cepa) and lisianthus necrosis in lisianthus (Eustoma russellianum). Characterization of virus isolates revealed genetic diversity among US, Brazilian, Dutch and Israeli isolates. IYSV was not seed transmitted, and in Israel, was not located in bulbs of infected plants. In the US, infected plants were generated from infected bulbs. The relationship between IYSV and Thrips tabaci was shown to be specific. Frankliniella occidentalis, the primary vector of many other tospoviruses, did not transmit IYSV isolates in Israel or the US. Furthermore, 1': tabaci populations varied in their transmission ability. Transmission was correlated to IYSV presence in thrips salivary glands. In Israel, surveys in onion fields revealed that the onion thrips, Thrips tabaci Lindeman was the predominant species and that its incidence was strongly related to that of IYSV infection. In contrast, in the U.S., T. tabaci and F. occidentalis were present in high numbers during the times sampled. In Israel, insecticides reduced onion thrips population and caused a significant yield increase. In the US, a genetic marker system that differentiates non-thrips transmissible isolates from thrips transmissible isolate demonstrated the importance of the M RNA to thrips transmission of tospoviruses. In addition, a symbiotic Erwinia was discovered in thrips and was shown to cause significant artifacts in certain types of virus binding experiments. Implications, scientific and agricultural. Rapid emergence of distinct tospoviruses and new vector relationships is profoundly important to global agriculture. We advanced the understanding of IYSV in bulb crops and its relationships with thrips vector species. The knowledge gained provided growers with new strategies for control and new tools for studying the importance of particular viral proteins in thrips specificity and transmission efficiency.
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