ArticleApplied and environmental microbiology2006
A Bacillus thuringiensis S-layer protein involved in toxicity against Epilachna varivestis (Coleoptera: Coccinellidae).
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 67 citations in OpenAlex.
- Therapeutic effect of GP543 strain of Bacillus thuringiensis against Amblyomma cajennense ticks in vitro and in naturally infested cattle.Parasitology research · 2024Article
- Diversity of transgenes in sustainable management of insect pests.Transgenic research · 2023Review
- Multiple S-Layer Proteins ofInternational journal of molecular sciences · 2023Article
- Insecticidal Activity ofToxins · 2020Review
- The Cytocidal Spectrum ofToxins · 2020Review
- Activity of Vip3Aa1 againstOpen life sciences · 2020Article
- Mass production of a S-layer protein of Bacillus thuringiensis and its toxicity to the cattle tick Rhipicephalus microplus.Scientific reports · 2019Article
- Efficacy of the vegetative cells of Lysinibacillus sphaericus for biological control of insecticide-resistant Aedes aegypti.Parasites & vectors · 2017Article
- Synergistic Activity Between S-Layer Protein and Spore-Crystal Preparations from Lysinibacillus sphaericus Against Culex quinquefasciatus Larvae.Current microbiology · 2017Article
- Acaricidal effect and histological damage induced by Bacillus thuringiensis protein extracts on the mite Psoroptes cuniculi.Parasites & vectors · 2015Article
- Article
- Contribution of S-layer proteins to the mosquitocidal activity of Lysinibacillus sphaericus.PloS one · 2014Article
- Article
- Proteomic analysis of Bacillus thuringiensis at different growth phases by using an automated online two-dimensional liquid chromatography-tandem mass spectrometry strategy.Applied and environmental microbiology · 2012Article
- Identification and functional analysis of the S-layer protein SplA of Paenibacillus larvae, the causative agent of American Foulbrood of honey bees.PLoS pathogens · 2012Article
- A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC.Journal of bacteriology · 2010Article
- Evaluation of Bacillus thuringiensis pathogenicity for a strain of the tick, Rhipicephalus microplus, resistant to chemical pesticides.Journal of insect science (Online) · 2010Article
- Characterization, identification, and cloning of the S-layer protein from Cytophaga sp.Current microbiology · 2008Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The use of Bacillus thuringiensis as a biopesticide is a viable alternative for insect control since the insecticidal Cry proteins produced by these bacteria are highly specific; harmless to humans, vertebrates, and plants; and completely biodegradable. In addition to Cry proteins, B. thuringiensis produces a number of extracellular compounds, including S-layer proteins (SLP), that contribute to virulence. The S layer is an ordered structure representing a proteinaceous paracrystalline array which completely covers the surfaces of many pathogenic bacteria. In this work, we report the identification of an S-layer protein by the screening of B. thuringiensis strains for activity against the coleopteran pest Epilachna varivestis (Mexican bean beetle; Coleoptera: Coccinellidae). We screened two B. thuringiensis strain collections containing unidentified Cry proteins and also strains isolated from dead insects. Some of the B. thuringiensis strains assayed against E. varivestis showed moderate toxicity. However, a B. thuringiensis strain (GP1) that was isolated from a dead insect showed a remarkably high insecticidal activity. The parasporal crystal produced by the GP1 strain was purified and shown to have insecticidal activity against E. varivestis but not against the lepidopteran Manduca sexta or Spodoptera frugiperda or against the dipteran Aedes aegypti. The gene encoding this protein was cloned and sequenced. It corresponded to an S-layer protein highly similar to previously described SLP in Bacillus anthracis (EA1) and Bacillus licheniformis (OlpA). The phylogenetic relationships among SLP from different bacteria showed that these proteins from Bacillus cereus, Bacillus sphaericus, B. anthracis, B. licheniformis, and B. thuringiensis are arranged in the same main group, suggesting similar origins. This is the first report that demonstrates that an S-layer protein is directly involved in toxicity to a coleopteran pest.
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