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Cadherin cry coleoptera

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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
#1
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/23645668/sodium-solute-symporter-and-cadherin-proteins-act-as-bacillus-thuringiensis-cry3ba-toxin-functional-receptors-in-tribolium-castaneum
#2
EstefanĂ­a 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/21495115/increased-toxicity-of-bacillus-thuringiensis-cry3aa-against-crioceris-quatuordecimpunctata-phaedon-brassicae-and-colaphellus-bowringi-by-a-tenebrio-molitor-cadherin-fragment
#3
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/19416969/a-novel-tenebrio-molitor-cadherin-is-a-functional-receptor-for-bacillus-thuringiensis-cry3aa-toxin
#4
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
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