Entomopathogenic Bacteria and Toxin: Utilization or Prevention?

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: closed (31 October 2024) | Viewed by 2332

Special Issue Editors


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Guest Editor
State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100094, China
Interests: Bacillus thuringiensis; toxin; insects; soil-borne disease

E-Mail Website
Guest Editor
State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100094, China
Interests: phylogenomics and diversity of bacteria; Bacillus thuringiensis; toxin; insects; soil-borne disease

Special Issue Information

Dear Colleagues,

In ecosystems, the relationship between insect pathogens, insects, and plants exhibits a subtle balance, making the ecosystem sustainable. However, in production practice, people have a direct view: if plants are products that people need, insect pathogenic bacteria (such as Bacillus thuringiensis) are used as insecticides to control pests; if insects are products that people need (such as resource insects), insect pathogenic bacteria are necessary to be controlled. Therefore, we need to study insect pathogens from ecological and applied perspectives. This Special Issue of Toxins mainly collects research papers and reviews on the following aspects:

  1. The interaction between insect pathogenic bacteria, toxins, insects, and plants;
  2. High-activity strain of Bacillus thuringiensis and new insecticidal active substances;
  3. New products, new formulations, and new application technologies of Bacillus thuringiensis;
  4. Non-Bt insect pathogenic bacteria toxins and their insecticidal mechanisms;
  5. Resource insects, pathogenic bacteria, toxins, and insecticidal mechanisms;
  6. Resource insects, pathogenic bacteria, toxins, and control techniques.

Dr. Changlong Shu
Dr. Lili Geng
Guest Editors

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Keywords

  • insect pathogenic bacteria
  • Bacillus thuringiensis toxins
  • insecticidal proteins

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Published Papers (2 papers)

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Research

12 pages, 1411 KiB  
Article
Scavenger Receptor C1 Mediates Toxicity of Binary Toxin from Lysinibacillus sphaericus to Ag55 Cells
by Qi Zhang, Gang Hua, Laramie Smith and Michael J. Adang
Toxins 2024, 16(8), 369; https://doi.org/10.3390/toxins16080369 - 21 Aug 2024
Viewed by 786
Abstract
Lysinibacillus sphaericus harboring Binary (BinA and BinB) toxins is highly toxic against Anopheles and Culex mosquito larvae. The Anopheles Ag55 cell line is a suitable model for investigating the mode of Bin toxin action. Based on the low-levels of α-glycosidase Agm3 mRNA in [...] Read more.
Lysinibacillus sphaericus harboring Binary (BinA and BinB) toxins is highly toxic against Anopheles and Culex mosquito larvae. The Anopheles Ag55 cell line is a suitable model for investigating the mode of Bin toxin action. Based on the low-levels of α-glycosidase Agm3 mRNA in Ag55 cells and the absence of detectable Agm3 proteins, we hypothesized that a scavenger receptor could be mediating Bin cytotoxicity. Preliminary RNA interference knockdown of the expressed scavenger receptors, combined with Bin cytotoxicity assays, was conducted. The scavenger Receptor C1 (SCRC1) became the focus of this study, as a putative receptor for Bin toxins in Ag55 cells, and SCRBQ2 was selected as a negative control. Open reading frames encoding SCRC1 and SCRBQ2 were cloned and expressed in vitro, and polyclonal antibodies were prepared for immunological analyses. The RNAi silencing of SCRC1 and SCRBQ2 resulted in the successful knockdown of both SCRC1 and SCRBQ2 transcripts and protein levels. The cytolytic toxicity of Bin against Ag55 cells was severely reduced after the SCRC1-RNAi treatment. The phagocytic receptor protein SCRC1 mediates endocytosis of the Bin toxin into Ag55 cells, thereby facilitating its internal cytological activity. The results support a mechanism of the Bin toxin entering Ag55 cells, possibly via SCRC1-mediated endocytosis, and encourage investigations into how Bin is transferred from its bound form on the midgut epithelial cells into the epithelial endocytic system. Full article
(This article belongs to the Special Issue Entomopathogenic Bacteria and Toxin: Utilization or Prevention?)
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13 pages, 5541 KiB  
Article
In Vivo and In Vitro Interactions between Exopolysaccharides from Bacillus thuringensis HD270 and Vip3Aa11 Protein
by Tianjiao Ma, Jinqiu Huang, Pengdan Xu, Changlong Shu, Zeyu Wang, Lili Geng and Jie Zhang
Toxins 2024, 16(5), 215; https://doi.org/10.3390/toxins16050215 - 7 May 2024
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Abstract
Bacillus thuringiensis (Bt) secretes the nutritional insecticidal protein Vip3Aa11, which exhibits high toxicity against the fall armyworm (Spodoptera frugiperda). The Bt HD270 extracellular polysaccharide (EPS) enhances the toxicity of Vip3Aa11 protoxin against S. frugiperda by enhancing the attachment of brush border [...] Read more.
Bacillus thuringiensis (Bt) secretes the nutritional insecticidal protein Vip3Aa11, which exhibits high toxicity against the fall armyworm (Spodoptera frugiperda). The Bt HD270 extracellular polysaccharide (EPS) enhances the toxicity of Vip3Aa11 protoxin against S. frugiperda by enhancing the attachment of brush border membrane vesicles (BBMVs). However, how EPS-HD270 interacts with Vip3Aa11 protoxin in vivo and the effect of EPS-HD270 on the toxicity of activated Vip3Aa11 toxin are not yet clear. Our results indicated that there is an interaction between mannose, a monosaccharide that composes EPS-HD270, and Vip3Aa11 protoxin, with a dissociation constant of Kd = 16.75 ± 0.95 mmol/L. When EPS-HD270 and Vip3Aa11 protoxin were simultaneously fed to third-instar larvae, laser confocal microscopy observations revealed the co-localization of the two compounds near the midgut wall, which aggravated the damage to BBMVs. EPS-HD270 did not have a synergistic insecticidal effect on the activated Vip3Aa11 protein against S. frugiperda. The activated Vip3Aa11 toxin demonstrated a significantly reduced binding capacity (548.73 ± 82.87 nmol/L) towards EPS-HD270 in comparison to the protoxin (34.96 ± 9.00 nmol/L). Furthermore, this activation diminished the affinity of EPS-HD270 for BBMVs. This study provides important evidence for further elucidating the synergistic insecticidal mechanism between extracellular polysaccharides and Vip3Aa11 protein both in vivo and in vitro. Full article
(This article belongs to the Special Issue Entomopathogenic Bacteria and Toxin: Utilization or Prevention?)
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