Identification of Henosepilachna vigintioctomaculata (Coleoptera: Coccinellidae) midgut putative receptor for Bacillus thuringiensis insecticidal Cry7Ab3 toxin

Song, Ping; Wang, Qinying; Nangong, Ziyan; Su, Junhong; DongHua, Ge

doi:10.1016/j.jip.2012.01.009

Cited by 25 publications

(25 citation statements)

References 27 publications

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“…These ultrastructural changes are similar to those widely described by other authors who worked with B. thuringiensis on different insect species including Lepidoptera (Endo and NishiitsutsujiUwo, 1980;Lane et al, 1989;Sousa et al, 2010;Abdelkefi-Mesrati et al, 2011), Diptera (Lacey and Federici, 1979;Lahkim-Tsoror et al, 1983;Dimitriadis and Domouhtsidou, 1996;Trona et al, 2004;Silva et al, 2008,) and Coleoptera (Bauer and Stuart Pankratz, 1992;Song et al, 2012). Comparable is the midgut deterioration determined by protein toxins from other entomopathogenic bacteria, such as B. sphaericus acting against mosquitoes (Davidson and Titus, 1987) or Xenorabdus nematophila against Helicoverpa armigera (Nangong et al, 2006).…”

Section: Discussionsupporting

confidence: 86%

Observations on house fly larvae midgut ultrastructure after Brevibacillus laterosporus ingestion

Ruiu

Satta

Floris

2012

Journal of Invertebrate Pathology

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Section: Discussionsupporting

confidence: 86%

Observations on house fly larvae midgut ultrastructure after Brevibacillus laterosporus ingestion

Ruiu

Satta

Floris

2012

Journal of Invertebrate Pathology

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“…A number of putative Bt protein receptors reported among other coleopterans include cadherin-like proteins [31], ADAM metalloprotease [32] and β-glucosidase [33], and in Lepidoptera include alkaline phosphatase, cadherin, aminopeptidase N, and ABC transporters [34]. In the current study, cadherin and amino peptidase N were not detected as DETs.…”

Section: Discussionmentioning

confidence: 51%

Patterns of Gene Expression in Western Corn Rootworm (Diabrotica virgifera virgifera) Neonates, Challenged with Cry34Ab1, Cry35Ab1 and Cry34/35Ab1, Based on Next-Generation Sequencing

Wang

Eyun

Arora³

et al. 2017

Toxins

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With Next Generation Sequencing technologies, high-throughput RNA sequencing (RNAseq) was conducted to examine gene expression in neonates of Diabrotica virgifera virgifera (LeConte) (Western Corn Rootworm, WCR) challenged with individual proteins of the binary Bacillus thuringiensis insecticidal proteins, Cry34Ab1 and Cry35Ab1, and the combination of Cry34/Cry35Ab1, which together are active against rootworm larvae. Integrated results of three different statistical comparisons identified 114 and 1300 differentially expressed transcripts (DETs) in the Cry34Ab1 and Cry34/35Ab1 treatment, respectively, as compared to the control. No DETs were identified in the Cry35Ab1 treatment. Putative Bt binding receptors previously identified in other insect species were not identified in DETs in this study. The majority of DETs (75% with Cry34Ab1 and 68.3% with Cry34/35Ab1 treatments) had no significant hits in the NCBI nr database. In addition, 92 DETs were shared between Cry34Ab1 and Cry34/35Ab1 treatments. Further analysis revealed that the most abundant DETs in both Cry34Ab1 and Cry34/35Ab1 treatments were associated with binding and catalytic activity. Results from this study confirmed the nature of these binary toxins against WCR larvae and provide a fundamental profile of expression pattern of genes in response to challenge of the Cry34/35Ab1 toxin, which may provide insight into potential resistance mechanisms.

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“…These differences could be attributed to differences in the experimental conditions used. The occurrence of two fragments after in vitro proteolytic processing was also described for another member of the Cry7 family (Cry7Ab3) and for members of other families, such as Cry1Ab, Cry3Aa, Cry8D, and Cry9Ca (31)(32)(33)(34)(35)(36)(37).…”

Section: Discussionmentioning

confidence: 91%

Shared Binding Sites for the Bacillus thuringiensis Proteins Cry3Bb, Cry3Ca, and Cry7Aa in the African Sweet Potato Pest Cylas puncticollis (Brentidae)

Hernández‐Martínez

Vera-Velasco

Martínez-Solís

et al. 2014

Appl Environ Microbiol

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bBacillus 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. Interestingly, processing of the 129-kDa Cry7Aa protoxin using commercial trypsin or chymotrypsin rendered two fragments of about 70 kDa and 65 kDa. N-terminal sequencing of the trypsin-activated Cry7Aa fragments revealed that processing occurs at Glu 47 for the 70-kDa form or Ile 88 for the 65-kDa form. Homologous binding assays showed specific binding of the two Cry3 proteins and the 65-kDa Cry7Aa fragment to brush border membrane vesicles (BBMV) from C. puncticollis larvae. The 70-kDa fragment did not bind to BBMV. Heterologous-competition assays showed that Cry3Bb, Cry3Ca, and Cry7Aa (65-kDa fragment) competed for the same binding sites. Hence, our results suggest that pest resistance mediated by the alteration of a shared Cry receptor binding site might render all three Cry toxins ineffective.

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Identification of Henosepilachna vigintioctomaculata (Coleoptera: Coccinellidae) midgut putative receptor for Bacillus thuringiensis insecticidal Cry7Ab3 toxin

Cited by 25 publications

References 27 publications

Observations on house fly larvae midgut ultrastructure after Brevibacillus laterosporus ingestion

Observations on house fly larvae midgut ultrastructure after Brevibacillus laterosporus ingestion

Patterns of Gene Expression in Western Corn Rootworm (Diabrotica virgifera virgifera) Neonates, Challenged with Cry34Ab1, Cry35Ab1 and Cry34/35Ab1, Based on Next-Generation Sequencing

Shared Binding Sites for the Bacillus thuringiensis Proteins Cry3Bb, Cry3Ca, and Cry7Aa in the African Sweet Potato Pest Cylas puncticollis (Brentidae)

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