The role of glycoconjugates as receptors for insecticidal proteins

Best, Hannah; Williamson, Lainey J.; Heath, Emily A.; Waller-Evans, Helen; Lloyd-Evans, Emyr; Berry, Colin

doi:10.1093/femsre/fuad026

Cited by 3 publications

(4 citation statements)

References 383 publications

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“…By contrast, Bt ‐Cry6Aa2 showed similar ineffectiveness as Bt ‐BMB171, the LC 50 of which was more than 100 ng μL −1 (Table S1). The solubilization of Bt toxin is the first step for recognition by pest receptors, and its solubilized form exhibited stronger toxicity against aphids in comparison with corresponding spore‐crystal mixture 35,36 . Therefore, the solubilized Cry5Ba2 and Cry6Aa2 was further used to confirm the toxicity to aphids.…”

Section: Resultsmentioning

confidence: 99%

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Resistance to both aphids and nematodes in tobacco plants expressing a Bacillus thuringiensis crystal protein

Wang,

Zhang

et al. 2024

Pest Management Science

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BACKGROUNDBacillus thuringiensis (Bt) and its crystal toxin or δ‐endotoxins (Cry) offer great potential for the efficient control of crop pests. A vast number of pests can potentially infect the same host plant, either simultaneously or sequentially. However, no effective Bt‐Cry protein has been reported to control both aphids and plant parasitic nematodes due to its highly specific activity.RESULTSOur study indicated that the Cry5Ba2 protein was toxic to the green peach aphid Myzus persicae, which had an LC50 of 9.7 ng μL−1 and fiducial limits of 3.1–34.6 ng/μL. Immunohistochemical localization of Cry5Ba2 revealed that it could bind to the apical tip of microvilli in midgut regions. Moreover, transgenic tobacco plants expressing Cry5Ba2 exhibited significant resistance to M. persicae, as evidenced by reduced insect survival and impaired fecundity, and also intoxicated the M. incognita as indicated by a decrease in galls and progeny reproduction.CONCLUSIONIn sum, we identified a new aphicidal Bt toxin resource that could simultaneously control both above‐ and below‐ground pests, thus extending the application range of Bt‐based strategy for crop protection.This article is protected by copyright. All rights reserved.

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Section: Resultsmentioning

confidence: 99%

“…Bt ‐Cry proteins have highly species‐specific activity, which are mainly determined by the receptor proteins and lipids in the midguts of target insects 36 . Glycosphingolipids have been identified as Cry5B receptors, they mediate toxicity in C. elegans 25,42,43 .…”

Section: Discussionmentioning

confidence: 99%

Resistance to both aphids and nematodes in tobacco plants expressing a Bacillus thuringiensis crystal protein

Wang,

Zhang

et al. 2024

Pest Management Science

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“…β-trefoil folds are highly conserved in the lectin family, a class of carbohydrate-binding proteins ( 28 ). Several studies have indicated a role for carbohydrate moieties in eliciting pesticidal action of Cry proteins ( 29 – 33 ). Hence, it is possible that carbohydrate binding may also be important for pesticidal activity of the Cry48Aa1/Tpp49Aa1 toxin pair.…”

Section: Resultsmentioning

confidence: 99%

Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

Williamson,

Galchenkova,

Best

et al. 2023

Proc. Natl. Acad. Sci. U.S.A.

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The Lysinibacillus sphaericus proteins Tpp49Aa1 and Cry48Aa1 can together act as a toxin toward the mosquito Culex quinquefasciatus and have potential use in biocontrol. Given that proteins with sequence homology to the individual proteins can have activity alone against other insect species, the structure of Tpp49Aa1 was solved in order to understand this protein more fully and inform the design of improved biopesticides. Tpp49Aa1 is naturally expressed as a crystalline inclusion within the host bacterium, and MHz serial femtosecond crystallography using the novel nanofocus option at an X-ray free electron laser allowed rapid and high-quality data collection to determine the structure of Tpp49Aa1 at 1.62 Å resolution. This revealed the packing of Tpp49Aa1 within these natural nanocrystals as a homodimer with a large intermolecular interface. Complementary experiments conducted at varied pH also enabled investigation of the early structural events leading up to the dissolution of natural Tpp49Aa1 crystals—a crucial step in its mechanism of action. To better understand the cooperation between the two proteins, assays were performed on a range of different mosquito cell lines using both individual proteins and mixtures of the two. Finally, bioassays demonstrated Tpp49Aa1/Cry48Aa1 susceptibility of Anopheles stephensi , Aedes albopictus, and Culex tarsalis larvae—substantially increasing the potential use of this binary toxin in mosquito control.

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“…The characterization studies of the midgut receptors for Cry toxins active to lepidopteran and dipteran larva, for instance, first identified cadherins, aminopeptidases, and alkaline phosphatases [8,64,65]. More recently, however, other molecules, such as ABC and ATP-binding cassette transporters, have been implied in their toxicity mechanism [66][67][68][69][70]. Further investigation is therefore necessary to evaluate any potential involvement of the Cx.…”

Section: Discussionmentioning

confidence: 99%

Culex quinquefasciatus Resistant to the Binary Toxin from Lysinibacillus sphaericus Displays a Consistent Downregulation of Pantetheinase Transcripts

Rezende,

Menezes,

Rezende

et al. 2023

Biomolecules

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Culex quinquefasciatus resistance to the binary (Bin) toxin, the major larvicidal component from Lysinibacillus sphaericus, is associated with mutations in the cqm1 gene, encoding the Bin-toxin receptor. Downregulation of the cqm1 transcript was found in the transcriptome of larvae resistant to the L. sphaericus IAB59 strain, which produces both the Bin toxin and a second binary toxin, Cry48Aa/Cry49Aa. Here, we investigated the transcription profiles of two other mosquito colonies having Bin resistance only. These confirmed the cqm1 downregulation and identified transcripts encoding the enzyme pantetheinase as the most downregulated mRNAs in both resistant colonies. Further quantification of these transcripts reinforced their strong downregulation in Bin-resistant larvae. Multiple genes were found encoding this enzyme in Cx. quinquefasciatus and a recombinant pantetheinase was then expressed in Escherichia coli and Sf9 cells, with its presence assessed in the midgut brush border membrane of susceptible larvae. The pantetheinase was expressed as a ~70 kDa protein, potentially membrane-bound, which does not seem to be significantly targeted by glycosylation. This is the first pantetheinase characterization in mosquitoes, and its remarkable downregulation might reflect features impacted by co-selection with the Bin-resistant phenotype or potential roles in the Bin-toxin mode of action that deserve to be investigated.

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The role of glycoconjugates as receptors for insecticidal proteins

Cited by 3 publications

References 383 publications

Resistance to both aphids and nematodes in tobacco plants expressing a Bacillus thuringiensis crystal protein

Resistance to both aphids and nematodes in tobacco plants expressing a Bacillus thuringiensis crystal protein

Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

Culex quinquefasciatus Resistant to the Binary Toxin from Lysinibacillus sphaericus Displays a Consistent Downregulation of Pantetheinase Transcripts

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