Mechanism of Cry1Ac resistance in cabbage loopers - a resistance mechanism selected in insect populations in an agricultural environment.

Wang, P.; Soberón, Mário; Gao, A.; Bravo, A.

doi:10.1079/9781780644370.0087

Cited by 2 publications

(3 citation statements)

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“…4 ). ALPs are important Bt receptors in the midgut of Cry-susceptible insects ( Perera et al 2009 , Wang 2015 ). Two CBRs ( 95 R- 102 G and 257 N- 296 I) were reported to play essential roles in mediating interaction of Cry-binding ALPs with Cry toxins ( Fernandez et al 2009 ).…”

Section: Resultsmentioning

confidence: 99%

“…Cry-receptor interaction is necessary for Cry toxin insecticidal activities to occur. It was observed that the deletion of putative Cry-receptor binding sites or low expression of specific receptor protein could significantly reduce the susceptibility of susceptible insects to the related Cry toxins ( Wang 2015 ). In addition, reinstallation of the dysfunctional receptor-binding domains of the resistant insect strains could restore the toxin insecticidal activity against the previously resistant insects ( Badran et al 2016 ).…”

Section: Discussionmentioning

confidence: 99%

“…The transcription abundance of bphCadherin, bphAPN, and bphALP was similar to that of their homologs in the midgut of Bt-susceptible insects ( Tiewsiri and Wang 2011 , Zhang et al 2012 , Chen et al 2015 ). Cry-binding cadherins, APNs, and ALPs were known as membrane-bound proteins ( Wang 2015 ). Prediction of transmembrane helix and GPI-anchored signal showed that bphAPN4, bphALP2, bphALP4, bphALP6, and all bphCadherins are potentially membrane-bound proteins with either GPI-anchor signal or transmembrane helix ( Table 1 ).…”

Section: Discussionmentioning

confidence: 99%

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Analysis of Homologs of Cry-toxin Receptor-Related Proteins in the Midgut of a Non-Bt Target, Nilaparvata lugens (Stål) (Hemiptera: Delphacidae)

Shao

Lin

Liu

et al. 2018

Journal of Insect Science

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The brown planthopper (BPH) Nilaparvata lugens is one of the most destructive insect pests in the rice fields of Asia. Like other hemipteran insects, BPH is not susceptible to Cry toxins of Bacillus thuringiensis (Bt) or transgenic rice carrying Bt cry genes. Lack of Cry receptors in the midgut is one of the main reasons that BPH is not susceptible to the Cry toxins. The main Cry-binding proteins (CBPs) of the susceptible insects are cadherin, aminopeptidase N (APN), and alkaline phosphatase (ALP). In this study, we analyzed and validated de novo assembled transcripts from transcriptome sequencing data of BPH to identify and characterize homologs of cadherin, APN, and ALP. We then compared the cadherin-, APN-, and ALP-like proteins of BPH to previously reported CBPs to identify their homologs in BPH. The sequence analysis revealed that at least one cadherin, one APN, and two ALPs of BPH contained homologous functional domains identified from the Cry-binding cadherin, APN, and ALP, respectively. Quantitative real-time polymerase chain reaction used to verify the expression level of each putative Cry receptor homolog in the BPH midgut indicated that the CBPs homologous APN and ALP were expressed at high or medium-high levels while the cadherin was expressed at a low level. These results suggest that homologs of CBPs exist in the midgut of BPH. However, differences in key motifs of CBPs, which are functional in interacting with Cry toxins, may be responsible for insusceptibility of BPH to Cry toxins.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%