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Bacillus thuringiensis receptor coleopteran

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https://www.readbyqxmd.com/read/27918112/validation-of-adam10-metalloprotease-as-a-bacillus-thuringiensis-cry3aa-toxin-functional-receptor-in-colorado-potato-beetle-leptinotarsa-decemlineata
#1
V M Ruiz-Arroyo, I García-Robles, C Ochoa-Campuzano, G A Goig, E Zaitseva, G Baaken, A C Martínez-Ramírez, C Rausell, M D Real
Bacillus thuringiensis parasporal crystal proteins (Cry proteins) are insecticidal pore-forming toxins that bind to specific receptor molecules on the brush border membrane of susceptible insect midgut cells to exert their toxic action. In the Colorado potato beetle (CPB), a coleopteran pest, we previously proposed that interaction of Cry3Aa toxin with a CPB ADAM10 metalloprotease is an essential part of the mode of action of this toxin. Here, we annotated the gene sequence encoding an ADAM10 metalloprotease protein (CPB-ADAM10) in the CPB genome sequencing project, and using RNA interference gene silencing we demonstrated that CPB-ADAM10 is a Cry3Aa toxin functional receptor in CPB...
December 5, 2016: Insect Molecular Biology
https://www.readbyqxmd.com/read/25957471/crystal-structure-of-cry51aa1-a-potential-novel-insecticidal-aerolysin-type-%C3%AE-pore-forming-toxin-from-bacillus-thuringiensis
#2
Chengchen Xu, Unmesh Chinte, Lirong Chen, Qingqing Yao, Ying Meng, Dayong Zhou, Li-Jun Bi, John Rose, Michael J Adang, Bi-Cheng Wang, Ziniu Yu, Ming Sun
The structures of several Bacillus thuringiensis (Bt) insecticidal crystal proteins have been determined by crystallographic methods and a close relationship has been explicated between specific toxicities and conserved three-dimensional architectures. In this study, as a representative of the coleopteran- and hemipteran-specific Cry51A group, the complete structure of Cry51Aa1 protoxin has been determined by X-ray crystallography at 1.65 Å resolution. This is the first report of a coleopteran-active Bt insecticidal toxin with high structural similarity to the aerolysin-type β-pore forming toxins (β-PFTs)...
July 3, 2015: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/25795679/identification-of-a-new-cry1i-type-gene-as-a-candidate-for-gene-pyramiding-in-corn-to-control-ostrinia-species-larvae
#3
Can Zhao, Juan Luis Jurat-Fuentes, Heba M Abdelgaffar, Hongyu Pan, Fuping Song, Jie Zhang
Pyramiding of diverse cry toxin genes from Bacillus thuringiensis with different modes of action is a desirable strategy to delay the evolution of resistance in the European corn borer (Ostrinia nubilalis). Considering the dependency of susceptibility to Cry toxins on toxin binding to receptors in the midgut of target pests, a diverse mode of action is commonly defined as recognition of unique binding sites in the target insect. In this study, we present a novel cry1Ie toxin gene (cry1Ie2) as a candidate for pyramiding with Cry1Ab or Cry1Fa in corn to control Ostrinia species larvae...
June 2015: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/25261517/shared-binding-sites-for-the-bacillus-thuringiensis-proteins-cry3bb-cry3ca-and-cry7aa-in-the-african-sweet-potato-pest-cylas-puncticollis-brentidae
#4
Patricia Hernández-Martínez, Natalia Mara Vera-Velasco, María Martínez-Solís, Marc Ghislain, Juan Ferré, Baltasar Escriche
Bacillus thuringiensis Cry3Bb, Cry3Ca, and Cry7Aa have been reported to be toxic against larvae of the genus Cylas, which are important pests of sweet potato worldwide and particularly in sub-Saharan Africa. However, relatively little is known about the processing and binding interactions of these coleopteran-specific Cry proteins. The aim of the present study was to determine whether Cry3Bb, Cry3Ca, and Cry7Aa proteins have shared binding sites in Cylas puncticollis to orient the pest resistance strategy by genetic transformation...
December 2014: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/25218400/a-coleopteran-cadherin-fragment-synergizes-toxicity-of-bacillus-thuringiensis-toxins-cry3aa-cry3bb-and-cry8ca-against-lesser-mealworm-alphitobius-diaperinus-coleoptera-tenebrionidae
#5
Youngjin Park, Gang Hua, Milton D Taylor, Michael J Adang
The lesser mealworm, Alphitobius diaperinus, is a serious cosmopolitan pest of commercial poultry facilities because of its involvement in structural damage to poultry houses, reduction in feed conversion efficiency, and transfer of avian and human pathogens. Cry3Aa, Cry3Bb, and Cry8Ca insecticidal proteins of Bacillus thuringiensis are used to control coleopteran larvae. Cadherins localized in the midgut epithelium function as receptors for Cry toxins in lepidopteran, coleopteran, and dipteran insects. Previously, we demonstrated that the truncated cadherin (DvCad1) from Diabrotica virgifera virgifera, which consists of the C-terminal cadherin repeats (CR) 8-10 and expressed in Escherichia coli, enhanced Cry3Aa and Cry3Bb toxicity against several coleopteran species...
November 2014: Journal of Invertebrate Pathology
https://www.readbyqxmd.com/read/24225445/cadherin-adcad1-in-alphitobius-diaperinus-larvae-is-a-receptor-of-cry3bb-toxin-from-bacillus-thuringiensis
#6
Gang Hua, Youngjin Park, Michael J Adang
Bacillus thuringiensis (Bt) Cry proteins are used as components of biopesticides or expressed in transgenic crops to control diverse insect pests worldwide. These Cry toxins bind to receptors on the midgut brush border membrane and kill enterocytes culminating in larval mortality. Cadherin proteins have been identified as Cry toxin receptors in diverse lepidopteran, coleopteran, and dipteran species. In the present work we report a 185 kDa cadherin (AdCad1) from larvae of the lesser mealworm (Alphitobius diaperinus) larvae as the first identified receptor for Cry3Bb toxin...
February 2014: Insect Biochemistry and Molecular Biology
https://www.readbyqxmd.com/read/23786046/bacillus-thuringiensis-insecticidal-crystal-proteins-affect-lifespan-and-reproductive-performance-of-helicoverpa-armigera-and-spodoptera-exigua-adults
#7
Ying Zhang, Yan Ma, Pin-Jun Wan, Li-Li Mu, Guo-Qing Li
Being delivered as sprays or expressed in plant, Bacillus thuringiensis (Bt) crystalline proteins (Cry toxins) display insecticidal activities against numerous Lepidopteran, Dipteran, and Coleopteran larvae. Comparative study of toxicities of Bt Cry toxins between larvae and adults may afford important new insights into the interactions of the toxins with receptor proteins in host insect, and represent intriguing targets for the control of insect pests. However, the effectiveness of Bt Cry toxins in insect adults has paid less attention...
April 2013: Journal of Economic Entomology
https://www.readbyqxmd.com/read/23645668/sodium-solute-symporter-and-cadherin-proteins-act-as-bacillus-thuringiensis-cry3ba-toxin-functional-receptors-in-tribolium-castaneum
#8
Estefanía Contreras, Michael Schoppmeier, M Dolores Real, Carolina Rausell
Understanding how Bacillus thuringiensis (Bt) toxins interact with proteins in the midgut of susceptible coleopteran insects is crucial to fully explain the molecular bases of Bt specificity and insecticidal action. In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sodium solute symporter (TcSSS) have been identified by ligand blot as putative Cry3Ba toxin-binding proteins in Tribolium castaneum (Tc) larvae. RNA interference knockdown of TcCad1 or TcSSS proteins resulted in decreased susceptibility to Cry3Ba toxin, demonstrating the Cry toxin receptor functionality for these proteins...
June 21, 2013: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/23541518/identification-of-a-bacillus-thuringiensis-cry8da-toxin-binding-glucosidase-from-the-adult-japanese-beetle-popillia-japonica
#9
Takuya Yamaguchi, Hisanori Bando, Shin-ichiro Asano
Cry8Da from Bacillus thuringiensis galleriae SDS-502 has insecticidal activity against both the larvae and adult Japanese beetle (Popillia japonica Newman). The receptor determines the specificity of the insecticidal activity of Cry proteins and hence, in order to reveal the mode of action of Cry toxin, receptor identification is a necessary step. However, a receptor for Cry8-type toxin has not been identified in the Scarabaeidae family of insects. Therefore, we aimed to identify the receptor of Cry8Da toxin in adult P...
June 2013: Journal of Invertebrate Pathology
https://www.readbyqxmd.com/read/23372850/proteome-response-of-tribolium-castaneum-larvae-to-bacillus-thuringiensis-toxin-producing-strains
#10
Estefanía Contreras, Carolina Rausell, M Dolores Real
Susceptibility of Tribolium castaneum (Tc) larvae was determined against spore-crystal mixtures of five coleopteran specific and one lepidopteran specific Bacillus thuringiensis Cry toxin producing strains and those containing the structurally unrelated Cry3Ba and Cry23Aa/Cry37Aa proteins were found toxic (LC(50) values 13.53 and 6.30 µg spore-crystal mixture/µL flour disc, respectively). Using iTRAQ combined with LC-MS/MS allowed the discovery of seven novel differentially expressed proteins in early response of Tc larvae to the two active spore-crystal mixtures...
2013: PloS One
https://www.readbyqxmd.com/read/23308139/bacillus-thuringiensis-cry34ab1-cry35ab1-interactions-with-western-corn-rootworm-midgut-membrane-binding-sites
#11
Huarong Li, Monica Olson, Gaofeng Lin, Timothy Hey, Sek Yee Tan, Kenneth E Narva
BACKGROUND: Bacillus thuringiensis (Bt) Cry34Ab1/Cry35Ab1 are binary insecticidal proteins that are co-expressed in transgenic corn hybrids for control of western corn rootworm, Diabrotica virgifera virgifera LeConte. Bt crystal (Cry) proteins with limited potential for field-relevant cross-resistance are used in combination, along with non-transgenic corn refuges, as a strategy to delay development of resistant rootworm populations. Differences in insect midgut membrane binding site interactions are one line of evidence that Bt protein mechanisms of action differ and that the probability of receptor-mediated cross-resistance is low...
2013: PloS One
https://www.readbyqxmd.com/read/21495115/increased-toxicity-of-bacillus-thuringiensis-cry3aa-against-crioceris-quatuordecimpunctata-phaedon-brassicae-and-colaphellus-bowringi-by-a-tenebrio-molitor-cadherin-fragment
#12
Yulin Gao, Juan Luis Jurat-Fuentes, Brenda Oppert, Jeffrey A Fabrick, Chenxi Liu, Jianhua Gao, Zhongren Lei
BACKGROUND: Biopesticides containing Cry insecticidal proteins from the bacterium Bacillus thuringiensis (Bt) are effective against many lepidopteran pests, but there is a lack of Bt-based pesticides for efficient control of important coleopteran pests. Based on the reported increase in Bt toxin oligomerization by a polypeptide from the Cry3Aa receptor cadherin in Tenebrio molitor (Coleoptera: Tenebrionidae), it was hypothesized that this cadherin peptide, rTmCad1p, would enhance Cry3Aa toxicity towards coleopteran larvae...
September 2011: Pest Management Science
https://www.readbyqxmd.com/read/21210704/multiple-receptors-as-targets-of-cry-toxins-in-mosquitoes
#13
Supaporn Likitvivatanavong, Jianwu Chen, Amy M Evans, Alejandra Bravo, Mario Soberon, Sarjeet S Gill
Bacillus thuringiensis (Bt) produces inclusions that are composed of proteins known as crystal proteins or Cry toxins. Due to their high specificity and their safety to humans and the environment, these Cry toxins are considered to be valuable alternatives to chemical pesticides in insect control programs. It is believed that Cry toxin-induced membrane pore formation is responsible for insect toxicity. The molecular mechanism of pore formation involves recognition and subsequent binding of the toxin to membrane receptors...
April 13, 2011: Journal of Agricultural and Food Chemistry
https://www.readbyqxmd.com/read/19416969/a-novel-tenebrio-molitor-cadherin-is-a-functional-receptor-for-bacillus-thuringiensis-cry3aa-toxin
#14
Jeff Fabrick, Cris Oppert, Marcé D Lorenzen, Kaley Morris, Brenda Oppert, Juan Luis Jurat-Fuentes
Cry toxins produced by the bacterium Bacillus thuringiensis are effective biological insecticides. Cadherin-like proteins have been reported as functional Cry1A toxin receptors in Lepidoptera. Here we present data that demonstrate that a coleopteran cadherin is a functional Cry3Aa toxin receptor. The Cry3Aa receptor cadherin was cloned from Tenebrio molitor larval midgut mRNA, and the predicted protein, TmCad1, has domain structure and a putative toxin binding region similar to those in lepidopteran cadherin B...
July 3, 2009: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/19329664/enhancement-of-bacillus-thuringiensis-cry3aa-and-cry3bb-toxicities-to-coleopteran-larvae-by-a-toxin-binding-fragment-of-an-insect-cadherin
#15
Youngjin Park, Mohd Amir F Abdullah, Milton D Taylor, Khalidur Rahman, Michael J Adang
The Cry3Aa and Cry3Bb insecticidal proteins of Bacillus thuringiensis are used in biopesticides and transgenic crops to control larvae of leaf-feeding beetles and rootworms. Cadherins localized in the midgut epithelium are identified as receptors for Cry toxins in lepidopteran and dipteran larvae. Previously, we discovered that a peptide of a toxin-binding cadherin expressed in Escherichia coli functions as a synergist for Cry1A toxicity against lepidopteran larvae and Cry4 toxicity against dipteran larvae...
May 2009: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/17147680/a-hybrid-bacillus-thuringiensis-delta-endotoxin-gives-resistance-against-a-coleopteran-and-a-lepidopteran-pest-in-transgenic-potato
#16
Samir Naimov, Stefan Dukiandjiev, Ruud A de Maagd
Expression of Bacillus thuringiensis delta-endotoxins has proven to be a successful strategy for obtaining insect resistance in transgenic plants. Drawbacks of expression of a single resistance gene are the limited target spectrum and the potential for rapid adaptation of the pest. Hybrid toxins with a wider target spectrum in combination with existing toxins may be used as tool to mitigate these problems. In this study, Desiree potato plants were genetically modified to resist attack by insect species belonging to the orders Coleoptera and Lepidoptera, through the insertion of such a hybrid gene, SN19...
January 2003: Plant Biotechnology Journal
https://www.readbyqxmd.com/read/14757225/role-of-toxin-activation-on-binding-and-pore-formation-activity-of-the-bacillus-thuringiensis-cry3-toxins-in-membranes-of-leptinotarsa-decemlineata-say
#17
COMPARATIVE STUDY
C Rausell, I García-Robles, J Sánchez, C Muñoz-Garay, A C Martínez-Ramírez, M D Real, A Bravo
Binding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis delta-endotoxins. In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin...
January 28, 2004: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/10812080/enhanced-toxicity-of-bacillus-thuringiensis-cry3a-delta-endotoxin-in-coleopterans-by-mutagenesis-in-a-receptor-binding-loop
#18
S J Wu, C N Koller, D L Miller, L S Bauer, D H Dean
We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 350-354. Two mutant toxins, A1 (R(345)A,Y(350)F,Y(351)F) and A2 (R(345)A,DeltaY(350), DeltaY(351)), showed significantly improved toxicity against Tenebrio molitor (yellow mealworm). The mutant toxin A1 was also more potent against both Leptinotarsa decemlineata (Colorado potato beetle) and Chrysomela scripta (cottonwood leaf beetle), while A2 displayed enhanced toxicity only in L. decemlineata. Competitive binding assays of L...
May 12, 2000: FEBS Letters
https://www.readbyqxmd.com/read/9614702/identification-of-bombyx-mori-midgut-receptor-for-bacillus-thuringiensis-insecticidal-cryia-a-toxin
#19
Y Nagamatsu, S Toda, F Yamaguchi, M Ogo, M Kogure, M Nakamura, Y Shibata, T Katsumoto
As part of a study of the mechanism by which Bacillus thuringiensis insecticidal crystal protein acts, a Bombyx mori receptor to the CryIA(a) toxin specific for lepidopterans was examined. Histological examination showed that the toxin acted on the brush-border membrane of the midgut columnar cells and broke its infolding structure, causing cell lysis. The membrane vesicles were purified, and a 175-kDa protein binding the toxin was found that accounted for some 0.015% of membrane proteins. The protein, designated BtR175, was a glycoprotein that reacted with concanavalin A...
April 1998: Bioscience, Biotechnology, and Biochemistry
https://www.readbyqxmd.com/read/8580914/brush-border-membrane-aminopeptidase-n-in-the-midgut-of-the-gypsy-moth-serves-as-the-receptor-for-the-cryia-c-delta-endotoxin-of-bacillus-thuringiensis
#20
A P Valaitis, M K Lee, F Rajamohan, D H Dean
Aminopeptidase-N (AP-N) was purified from gypsy moth (Lymantria dispar, L.) brush border membrane vesicles (BBMV) proteins by mono-Q chromatography and Superdex-75 gel filtration in the presence of the zwitterionic detergent, CHAPS, using FPLC. The purified AP-N, identified by its enzymatic activity, had an apparent size of 100 kDa, and was identified as the unique Bacillus thuringiensis insecticidal toxin, CryIA(c), binding protein. AP-N clearly displayed strong binding to CryIA(c), exhibiting little or no binding to CryIA(a) or CryIA(b), and showing no binding for the coleopteran-specific toxin, CryIIIA...
December 1995: Insect Biochemistry and Molecular Biology
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