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cadherine coleoptera

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https://www.readbyqxmd.com/read/27334721/rnai-induced-knockdown-of-a-cadherin-like-protein-ef531715-does-not-affect-toxicity-of-cry34-35ab1-or-cry3aa-to-diabrotica-virgifera-virgifera-larvae-coleoptera-chrysomelidae
#1
Sek Yee Tan, Murugesan Rangasamy, Haichuan Wang, Ana María Vélez, James Hasler, David McCaskill, Tao Xu, Hong Chen, Jessica Jurzenski, Matthew Kelker, Xiaoping Xu, Kenneth Narva, Blair D Siegfried
The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is an important maize pest throughout most of the U.S. Corn Belt. Bacillus thuringiensis (Bt) insecticidal proteins including modified Cry3Aa and Cry34/35Ab1 have been expressed in transgenic maize to protect against WCR feeding damage. To date, there is limited information regarding the WCR midgut target sites for these proteins. In this study, we examined whether a cadherin-like gene from Diabrotica virgifera virgifera (DvvCad; GenBank accession # EF531715) associated with WCR larval midgut tissue is necessary for Cry3Aa or Cry34/35Ab1 toxicity...
August 2016: Insect Biochemistry and Molecular Biology
https://www.readbyqxmd.com/read/26313197/evaluation-of-reference-genes-for-rt-qpcr-in-tribolium-castaneum-coleoptera-tenebrionidae-under-uvb-stress
#2
Wen Sang, Li He, Xiao-Ping Wang, Keyan Zhu-Salzman, Chao-Liang Lei
Reverse transcriptase quantitative polymerase chain reaction (RT-qPCR) has become a widely used technique to quantify gene expression. It is necessary to select appropriate reference genes for normalization. In the present study, we assessed the expression stability of seven candidate genes in Tribolium castaneum (Herbst) (Coleoptera: Tenebrionidae) irradiated by ultraviolet B (UVB) at different developmental stages for various irradiation time periods. The algorithms of geNorm, NormFinder, and BestKeeper were applied to determine the stability of these candidate genes...
April 2015: Environmental Entomology
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
#3
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
#4
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/22306353/identification-of-henosepilachna-vigintioctomaculata-coleoptera-coccinellidae-midgut-putative-receptor-for-bacillus-thuringiensis-insecticidal-cry7ab3-toxin
#5
Ping Song, QinYing Wang, ZiYan Nangong, JunPing Su, DongHua Ge
Bt WZ-9 strain, containing a single Cry7Ab3 toxin, had effective insecticidal activity against larvae of Henosepilachna vigintioctomaculata. By incubation with larvae midgut homogenate and trypsin in vitro, 130 kDa Cry7Ab3 protoxin was degraded into the ∼75 kDa proteinase-resistant fragments. In vivo analysis, 130 kDa Cry7Ab3 protoxin was also processed into ∼75 kDa fragment. Histopathological observations indicated that Cry7Ab3 ingestion by H. vigintioctomaculata larvae causes acceleration in the blebbing of the midgut epithelium cells into the gut lumen and eventual lysis of the epithelium cells resulting in larval death...
March 2012: Journal of Invertebrate Pathology
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
#6
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
#7
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/19364528/pyrosequencing-of-the-midgut-transcriptome-of-the-poplar-leaf-beetle-chrysomela-tremulae-reveals-new-gene-families-in-coleoptera
#8
Yannick Pauchet, Paul Wilkinson, Manuella van Munster, Sylvie Augustin, David Pauron, Richard H ffrench-Constant
The insect midgut is the primary target site for Bt-derived insecticides and Bt alternatives. However, despite extensive recent study, the precise role and nature of different Bt receptors remains a subject of considerable debate. This problem is fuelled by a lack of understanding of the genes expressed in the insect midgut and their physiological roles. The poplar leaf beetle, Chrysomela tremulae, is an important model for understanding the mode of action of, and resistance to, coleopteran-specific Bt toxins and currently shows the only known naturally occurring case of resistance to Cry3A toxins...
May 2009: Insect Biochemistry and Molecular Biology
https://www.readbyqxmd.com/read/17725800/a-novel-cadherin-like-gene-from-western-corn-rootworm-diabrotica-virgifera-virgifera-coleoptera-chrysomelidae-larval-midgut-tissue
#9
A Sayed, E R Nekl, H A A Siqueira, H-C Wang, R H Ffrench-Constant, M Bagley, B D Siegfried
A cadherin-like gene associated with larval midgut tissues was cloned from western corn rootworm (Diabrotica virgifera virgifera: Coleoptera), an economically important agricultural pest in North America and Europe and the primary target pest species for corn hybrids expressing Cry3 toxins from Bacillus thuringiensis (Bt). The full-length cDNA (5371 bp in length) encodes an open reading frame for a 1688 amino acid polypeptide. The putative protein has similar architecture to cadherin-like proteins isolated from lepidopteran midguts that have been shown to bind to Cry1 Bt toxins and have been implicated in Bt resistance...
October 2007: Insect Molecular Biology
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