Autophagy induced by Vip3Aa has a pro-survival role in <i>Spodoptera frugiperda</i> Sf9 cells

Hou, Xiaoyue; Han, Lu; An, Baoju; Cai, Jin

doi:10.1080/21505594.2021.1878747

Cited by 9 publications

(7 citation statements)

References 35 publications

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“…The results here do not support a substantial role in the resistance of DH-R to Vip3Aa for six genes previously reported to affect responses to Vip3Aa in S. frugiperda ( 46 – 50 ). In previous work with S. frugiperda , using CRISPR/Cas9 to knock out the gene encoding the receptor protein ABCC2 caused resistance to Cry1Ab and Cry1Fa ( 37 , 51 , 52 ) but CRISPR/Cas9 KOs of scavenger receptor-C or fibroblast growth factor receptor did not affect susceptibility to Vip3Aa ( 53 ).…”

Section: Discussioncontrasting

confidence: 99%

“…It has recently invaded Africa, Asia, and Australia ( 44 ), and it has evolved practical resistance in the Americas to the Cry toxins in Bt crops ( 12 , 45 ). Previous work with S. frugiperda has identified three putative receptors for Vip3Aa and three proteins putatively involved in defense against Vip3Aa ( 46 – 50 ), but we are not aware of any evidence linking these proteins with resistance to Vip3Aa selected in the laboratory or field. Here, we report the identification of an association between resistance to Vip3Aa in S. frugiperda and downregulation of a transcription factor gene for which no role in Bt toxicity has been reported before.…”

mentioning

confidence: 73%

“…We evaluated the potential role in resistance to Vip3Aa of three S. frugiperda genes encoding proteins that putatively defend against Vip3Aa ( autophagy related gene 5 , phenyloxidase-activating enzyme-like , phenyloxidase subunit 2-like ) and three encoding putative Vip3Aa receptors ( scavenger receptor-C , fibroblast growth factor receptor , and ribosomal S2 ) ( 46 – 50 ). In the GWAS we conducted, these six genes were not associated with resistance to Vip3Aa ( Fig.…”

Section: Resultsmentioning

confidence: 99%

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Downregulation of a transcription factor associated with resistance to Bt toxin Vip3Aa in the invasive fall armyworm

Jin,

Shan,

Peng

et al. 2023

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

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Transgenic crops producing insecticidal proteins from Bacillus thuringiensis (Bt) have revolutionized control of some major pests. However, more than 25 cases of field-evolved practical resistance have reduced the efficacy of transgenic crops producing crystalline (Cry) Bt proteins, spurring adoption of alternatives including crops producing the Bt vegetative insecticidal protein Vip3Aa. Although practical resistance to Vip3Aa has not been reported yet, better understanding of the genetic basis of resistance to Vip3Aa is urgently needed to proactively monitor, delay, and counter pest resistance. This is especially important for fall armyworm ( Spodoptera frugiperda ), which has evolved practical resistance to Cry proteins and is one of the world’s most damaging pests. Here, we report the identification of an association between downregulation of the transcription factor gene SfMyb and resistance to Vip3Aa in S. frugiperda . Results from a genome-wide association study, fine-scale mapping, and RNA-Seq identified this gene as a compelling candidate for contributing to the 206-fold resistance to Vip3Aa in a laboratory-selected strain. Experimental reduction of SfMyb expression in a susceptible strain using RNA interference (RNAi) or CRISPR/Cas9 gene editing decreased susceptibility to Vip3Aa, confirming that reduced expression of this gene can cause resistance to Vip3Aa. Relative to the wild-type promoter for SfMyb , the promoter in the resistant strain has deletions and lower activity. Data from yeast one-hybrid assays, genomics, RNA-Seq, RNAi, and proteomics identified genes that are strong candidates for mediating the effects of SfMyb on Vip3Aa resistance. The results reported here may facilitate progress in understanding and managing pest resistance to Vip3Aa.

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Section: Discussioncontrasting

confidence: 99%

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confidence: 73%

Section: Resultsmentioning

confidence: 99%

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Downregulation of a transcription factor associated with resistance to Bt toxin Vip3Aa in the invasive fall armyworm

Jin,

Shan,

Peng

et al. 2023

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

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“…It has been reported that Vip3 protein attacked the lysosome, reduced its membrane stability, and hampered the degradation of the autophagosome (Hou et al, 2020). The Vip3Aa-induced autophagy in Sf9 cells of S. frugiperda was also confirmed through the presence of autophagic vacuoles and increased level of protein Atg8-II (Hou et al, 2021). It was found that autophagy in Sf9 cells caused by this toxic protein was mediated through the AMPK-mTOR-ULK1 pathway associated with disruption of ATP-homeostasis in treated cells.…”

Section: Autophagymentioning

confidence: 82%

Vegetative Insecticidal Protein (Vip): A Potential Contender From Bacillus thuringiensis for Efficient Management of Various Detrimental Agricultural Pests

2021

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Bacillus thuringiensis (Bt) bacterium is found in various ecological habitats, and has natural entomo-pesticidal properties, due to the production of crystalline and soluble proteins during different growth phases. In addition to Cry and Cyt proteins, this bacterium also produces Vegetative insecticidal protein (Vip) during its vegetative growth phase, which is considered an excellent toxic candidate because of the difference in sequence homology and receptor sites from Cry proteins. Vip proteins are referred as second-generation insecticidal proteins, which can be used either alone or in complementarity with Cry proteins for the management of various detrimental pests. Among these Vip proteins, Vip1 and Vip2 act as binary toxins and have toxicity toward pests belonging to Hemiptera and Coleoptera orders, whereas the most important Vip3 proteins have insecticidal activity against Lepidopteran pests. These Vip3 proteins are similar to Cry proteins in terms of toxicity potential against susceptible insects. They are reported to be toxic toward pests, which can’t be controlled with Cry proteins. The Vip3 proteins have been successfully pyramided along with Cry proteins in transgenic rice, corn, and cotton to combat resistant pest populations. This review provides detailed information about the history and importance of Vip proteins, their types, structure, newly identified specific receptors, and action mechanism of this specific class of proteins. Various studies conducted on Vip proteins all over the world and the current status have been discussed. This review will give insights into the significance of Vip proteins as alternative promising candidate toxic proteins from Bt for the management of pests in most sustainable manner.

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“…However, only Cry proteins have been extensively studied and successfully used worldwide 7,8, 13–15, 17, 51, 52 . Vip3 proteins have characteristics and mode-of-action mechanisms distinct from Cry proteins and show high insecticidal activity against lepidopteran pests and are classified as a second generation of insecticidal proteins that can be broadly applied after Cry proteins in the field 3, 22, 24, 25, 53 . However, the lack of clear understanding of the molecular mechanisms underlying their insecticidal activity severely restricts their broader application and rational development.…”

Section: Discussionmentioning

confidence: 99%

Functional characterization of multidomain protein Vip3Aa from Bacillus thuringiensis reveals a strategy to increase its insecticidal potency

Jiang

Chen

Shi

et al. 2022

Preprint

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Microbially derived, protein-based biopesticides offer a more sustainable pest management alternative to synthetic pesticides. Vegetative insecticidal proteins (Vip3), multidomain proteins secreted by Bacillus thuringiensis, represent a second-generation insecticidal toxin that have been used in transgenic crops. However, the molecular mechanism underlying Vip3's toxicity is poorly understood. Here, we determine the distinct functions and contributions of the domains of the Vip3Aa protein to its toxicity against Spodoptera frugiperda larvae. Vip3Aa domains II and III (DII-DIII) bind the midgut epithelium, while DI maintains the tetrameric state of the Vip3Aa protoxin, which is essential for its stability and toxicity. DI-DIII can be activated by midgut proteases, and exhibits ex vivo cytotoxicity similar to full-length Vip3Aa. We also determine that DV binds the peritrophic matrix via its glycan-binding activity, which is essential for Vip3Aa insecticidal activity. We further show that Vip3Aa has multiple protease activation sites and that introducing additional cleavage sites between DI and DII can increase the proteolysis efficiency and boost Vip3Aa insecticidal potency. This study provides insights into Vip3Aa's mode-of-action and demonstrates a proof-of-concept strategy to enhance the insecticidal potency of Vip3Aa, which should significantly improve its application and development as a biopesticide.

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Autophagy induced by Vip3Aa has a pro-survival role in Spodoptera frugiperda Sf9 cells

Cited by 9 publications

References 35 publications

Downregulation of a transcription factor associated with resistance to Bt toxin Vip3Aa in the invasive fall armyworm

Downregulation of a transcription factor associated with resistance to Bt toxin Vip3Aa in the invasive fall armyworm

Vegetative Insecticidal Protein (Vip): A Potential Contender From Bacillus thuringiensis for Efficient Management of Various Detrimental Agricultural Pests

Functional characterization of multidomain protein Vip3Aa from Bacillus thuringiensis reveals a strategy to increase its insecticidal potency

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