Mechanistic insights into the first Lygus-active β-pore forming protein

Jerga, Agoston; Chen, Danqi; Zhang, Chunfen; Fu, Jinping; Kouadio, Jean-Louis K.; Wang, Yanfei; Duff, Stephen M. G.; Howard, Jennifer; Rydel, T.J.; Evdokimov, A.G.; Parthasarathy, R.; Evans, Adam; Bolognesi, Renata; Park, Yoonseong; Haas, Jeffrey A.

doi:10.1016/j.abb.2016.03.016

Cited by 22 publications

(42 citation statements)

References 32 publications

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“…The specificity of the protein—and therefore selective activity against insects—of these Bt proteins is believed to derive from a combination of their relative solubility, stability, proteolytic activation, and receptor binding on the insect midgut epithelium [35]. Jerga et al, [34] recently confirmed that the mode of action of the Cry51Aa2.834_16 protein follows the same general steps as other Bt Cry proteins, including proteolytic activation, dimer dissociation, specific binding to brush border membranes and damage of the Lygus midgut [34]. …”

Section: Discussionmentioning

confidence: 99%

“…In brief, the biological activity and specificity of Cry51Aa2.834_16 is the result of the combined effects of achieving solubilization after ingestion of the protein by the target insect(s), proteolytic activation, binding to specific receptors on the insect midgut cell membrane, oligomerization, and pore formation [34, 35]. A more in depth discussion of the MoA of the Cry51Aa2.834_16 protein is provided in Jerga et al, [34]. Importantly, it is the combination of all of these steps (ingestion, activation and receptor-binding) that are required for activity, and thus result in a high degree of specificity [36].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

et al. 2017

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The spectrum of insecticidal activity of Cry51Aa2.834_16 protein targeting hemipteran and thysanopteran insect pests in cotton was characterized by selecting and screening multiple pest and non-pest species, based on representation of ecological functional groups, taxonomic relatedness (e.g. relationship to species where activity was observed), and availability for effective testing. Seven invertebrate orders, comprising 12 families and 17 representative species were screened for susceptibility to Cry51Aa2.834_16 protein and/or the ability of the protein to protect against feeding damage in laboratory, controlled environments (e.g. greenhouse/growth chamber), and/or field studies when present in cotton plants. The screening results presented for Cry51Aa2.834_16 demonstrate selective and limited activity within three insect orders. Other than Orius insidiosus, no activity was observed for Cry51Aa2.834_16 against several groups of arthropods that perform key ecological roles in some agricultural ecosystems (e.g. pollinators, decomposers, and natural enemies).

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

et al. 2017

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“…The insoluble debris was pelleted, and the full-length proteins were subjected to trypsinization and follow-up purification on a Q-Sepharose anion exchange column. Intact molecular weight determination using quadrupole time of flight liquid chromatography-mass spectrometry (Q-TOF LC-MS) provided the weight difference between full-length and truncated forms of the protein and was used to assess the N and C termini of the activated protein core (68). Spot densitometry using a bovine serum albumin (BSA) standard on SDS-PAGE gels was used to quantitate the protein samples.…”

Section: Methodsmentioning

confidence: 99%

Bacillus thuringiensis Cry1Da_7 and Cry1B.868 Protein Interactions with Novel Receptors Allow Control of Resistant Fall Armyworms, Spodoptera frugiperda (J.E. Smith)

Wang

et al. 2019

Appl Environ Microbiol

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Two new modified Bacillus thuringiensis (Bt) proteins, Cry1Da_7 and Cry1B.868, with activity against fall armyworms (FAW), Spodoptera frugiperda (J.E. Smith), were evaluated for their potential to bind new insect receptors compared to proteins currently deployed as plant-incorporated protectants (PIPs) in row crops. Results from resistant insect bioassays, disabled insecticidal protein (DIP) bioassays, and cell-based assays using insect cells expressing individual receptors demonstrate that receptor utilizations of the newly modified Cry1Da_7 and Cry1B.868 proteins are distinct from each other and from those of commercially available Bt proteins such as Cry1F, Cry1A.105, Cry2Ab, and Vip3A. Accordingly, these two proteins target different insect proteins in FAW midgut cells and when pyramided together should provide durability in the field against this economically important pest. IMPORTANCE There is increased concern with the development of resistance to insecticidal proteins currently expressed in crop plants, especially against high-resistance-risk pests such as fall armyworm (FAW), Spodoptera frugiperda, a maize pest that already has developed resistance to Bacillus thuringiensis (Bt) proteins such as Cry1F. Lepidopteran-specific proteins that bind new insect receptors will be critical in managing current Cry1F-resistant FAW and delaying future resistance development. Results from resistant insect assays, disabled insecticidal protein (DIP) bioassays, and cell-based assays using insect cells expressing individual receptors demonstrate that target receptors of the Cry1Da_7 and Cry1B.868 proteins are different from each other and from those of commercially available Bt proteins such as Cry1F, Cry1A.105, Cry2Ab, and Vip3A. Therefore, pyramiding these two new proteins in maize will provide durable control of this economically important pest in production agriculture.

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“…In recent years, the trend is to include multiple genes of interest within a single DNA construct (Weber et al, 2012;NAS, 2016). For example, for effective insect control, different mechanisms of action can be identified by a combination of competitive binding experiments and testing new control agents against insects resistant to other insecticides (Pardo-López et al, 2013;Ladics et al, 2015aLadics et al, , 2015bChakroun et al, 2016;Jerga A et al, 2016;Jurat-Fuentes and Crickmore, 2017;Moar et al, 2017). Typically, dozens of versions of an expression cassette are tested in plants, both in greenhouse and confined field trials, to determine which best optimizes the gene expression needed to ensure commercial viability and reproducible efficacy of the trait.…”

Section: Breeding Of Gm Crops Sources Of Candidate Genes For Gm Cropsmentioning

confidence: 99%

Bringing New Plant Varieties to Market: Plant Breeding and Selection Practices Advance Beneficial Characteristics while Minimizing Unintended Changes

et al. 2017

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Commercial‐scale plant breeding is a complex process in which new crop varieties are continuously being developed to improve yield and agronomic performance over current varieties. A wide array of naturally occurring genetic changes are sources of new characteristics available to plant breeders. During conventional plant breeding, genetic material is exchanged that has the potential to beneficially or adversely affect plant characteristics. For this reason, commercial‐scale breeders have implemented extensive plant selection practices to identify the top‐performing candidates with the desired characteristics while minimizing the advancement of unintended changes. Selection practices in maize (Zea mays L.) breeding involve phenotypic assessments of thousands of candidate lines throughout hundreds of different environmental conditions over many years. Desirable characteristics can also be introduced through genetic modification. For genetically modified (GM) crops, molecular analysis is used to select transformed plants with a single copy of an intact DNA insert and without disruption of endogenous genes. All the while, GM crops go through the same extensive phenotypic characterization as conventionally bred crops. Data from both conventional and GM maize breeding programs are presented to show the similarities between these two processes.

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Mechanistic insights into the first Lygus-active β-pore forming protein

Cited by 22 publications

References 32 publications

Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

Bacillus thuringiensis Cry1Da_7 and Cry1B.868 Protein Interactions with Novel Receptors Allow Control of Resistant Fall Armyworms, Spodoptera frugiperda (J.E. Smith)

Bringing New Plant Varieties to Market: Plant Breeding and Selection Practices Advance Beneficial Characteristics while Minimizing Unintended Changes

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