Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action
Bacillus thuringiensis (Bt)-based products are the most successful microbial insecticides to date. This entomopathogenic bacterium produces different kinds of proteins whose specific toxicity has been shown against a wide range of insect orders, nematodes, mites, protozoa, and human cancer cells. So...
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MDPI - Multidisciplinary Digital Publishing Institute
2022
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| Online toegang: | ONIX_20220111_9783036520490_851 |
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| description | Bacillus thuringiensis (Bt)-based products are the most successful microbial insecticides to date. This entomopathogenic bacterium produces different kinds of proteins whose specific toxicity has been shown against a wide range of insect orders, nematodes, mites, protozoa, and human cancer cells. Some of these proteins are accumulated in parasporal crystals during the sporulation phase (Cry and Cyt proteins), whereas other proteins are secreted in the vegetative phase of growth (Vip and Sip toxins). Currently, insecticidal proteins belonging to different groups (Cry and Vip3 proteins) are widely used to control insect pests and vectors both in formulated sprays and in transgenic crops (the so-called Bt crops). Despite the extensive use of these proteins in insect pest control, especially Cry and Vip3, their mode of action is not completely understood. The aim of this Special Issue was to gather information that could summarize (in the form of review papers) or expand (research papers) the knowledge of the structure and function of Bt proteins, as well as shed light on their mode of action, especially regarding the insect receptors. This subject has generated great interest, and this interest has been materialized into the 18 papers of important scientific value in the field (5 reviews and 13 research papers) that have been compiled in this issue. |
| format | Online |
| id | doab-20.500.12854ir-77019 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2022 |
| publishDateRange | 2022 |
| publishDateSort | 2022 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
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| spelling | doab-20.500.12854ir-770192024-03-27T16:34:43Z Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action Bel, Yolanda Ferré, Juan Hernández-Martínez, Patricia Bacillus thuringiensis Plutella xylostella Cry1Ac resistance trypsin-like midgut protease protoxin activation Spodoptera spp., Helicoverpa armigera Mamestra brassicae Anticarsia gemmatalis Ostrinia furnacalis Cry2Ab toxin Bombyx mori ATP-binding cassette subfamily a member 2 (ABCA2) genome editing transcription activator-like effector-nucleases (TALENs) HEK293T cell functional receptor Vip3Aa lysosome mitochondria apoptosis Sf9 cells Cry1Ab oligomer formation Sf21 cell line Ostrinia nubilalis Lobesia botrana Leptinotarsa decemlineata bioassay Cyt2Aa2 toxin protein-lipid binding erythrocyte membrane AFM QCM-D Asian corn borer ABCC2 CRISPR/Cas9 Cry1Fa resistance chitin-binding protein adhesion peritrophic matrix Vip3A Spodoptera litura site-directed mutagenesis Cry Cyt parasporins S-layer proteins Vip Sip membrane receptors insecticidal activity anticancer activity Aedes aegypti minor proteins synergy mosquito control Bti Spodoptera frugiperda cadherin mode of action of Cry toxin insecticidal proteins insect resistance tobacco budworm Bacillus thuringiensis proteins coleopteran pests structure mode of action 3D-structure biological control antimicrobial peptide gut microbiota vegetative insecticidal proteins pyramids 3D-Cry toxins in vitro evolution rational design toxin enhancement n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general Bacillus thuringiensis (Bt)-based products are the most successful microbial insecticides to date. This entomopathogenic bacterium produces different kinds of proteins whose specific toxicity has been shown against a wide range of insect orders, nematodes, mites, protozoa, and human cancer cells. Some of these proteins are accumulated in parasporal crystals during the sporulation phase (Cry and Cyt proteins), whereas other proteins are secreted in the vegetative phase of growth (Vip and Sip toxins). Currently, insecticidal proteins belonging to different groups (Cry and Vip3 proteins) are widely used to control insect pests and vectors both in formulated sprays and in transgenic crops (the so-called Bt crops). Despite the extensive use of these proteins in insect pest control, especially Cry and Vip3, their mode of action is not completely understood. The aim of this Special Issue was to gather information that could summarize (in the form of review papers) or expand (research papers) the knowledge of the structure and function of Bt proteins, as well as shed light on their mode of action, especially regarding the insect receptors. This subject has generated great interest, and this interest has been materialized into the 18 papers of important scientific value in the field (5 reviews and 13 research papers) that have been compiled in this issue. 2022-01-11T13:49:29Z 2022-01-11T13:49:29Z 2021 book ONIX_20220111_9783036520490_851 9783036520490 9783036520506 https://directory.doabooks.org/handle/20.500.12854/77019 eng image/jpeg Attribution 4.0 International https://mdpi.com/books/pdfview/book/4629 https://mdpi.com/books/pdfview/book/4629 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-2050-6 10.3390/books978-3-0365-2050-6 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036520490 9783036520506 340 Basel, Switzerland open access |
| spellingShingle | Bacillus thuringiensis Plutella xylostella Cry1Ac resistance trypsin-like midgut protease protoxin activation Spodoptera spp., Helicoverpa armigera Mamestra brassicae Anticarsia gemmatalis Ostrinia furnacalis Cry2Ab toxin Bombyx mori ATP-binding cassette subfamily a member 2 (ABCA2) genome editing transcription activator-like effector-nucleases (TALENs) HEK293T cell functional receptor Vip3Aa lysosome mitochondria apoptosis Sf9 cells Cry1Ab oligomer formation Sf21 cell line Ostrinia nubilalis Lobesia botrana Leptinotarsa decemlineata bioassay Cyt2Aa2 toxin protein-lipid binding erythrocyte membrane AFM QCM-D Asian corn borer ABCC2 CRISPR/Cas9 Cry1Fa resistance chitin-binding protein adhesion peritrophic matrix Vip3A Spodoptera litura site-directed mutagenesis Cry Cyt parasporins S-layer proteins Vip Sip membrane receptors insecticidal activity anticancer activity Aedes aegypti minor proteins synergy mosquito control Bti Spodoptera frugiperda cadherin mode of action of Cry toxin insecticidal proteins insect resistance tobacco budworm Bacillus thuringiensis proteins coleopteran pests structure mode of action 3D-structure biological control antimicrobial peptide gut microbiota vegetative insecticidal proteins pyramids 3D-Cry toxins in vitro evolution rational design toxin enhancement n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action |
| title | Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action |
| title_full | Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action |
| title_fullStr | Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action |
| title_full_unstemmed | Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action |
| title_short | Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action |
| title_sort | bacillus thuringiensis toxins functional characterization and mechanism of action |
| topic | Bacillus thuringiensis Plutella xylostella Cry1Ac resistance trypsin-like midgut protease protoxin activation Spodoptera spp., Helicoverpa armigera Mamestra brassicae Anticarsia gemmatalis Ostrinia furnacalis Cry2Ab toxin Bombyx mori ATP-binding cassette subfamily a member 2 (ABCA2) genome editing transcription activator-like effector-nucleases (TALENs) HEK293T cell functional receptor Vip3Aa lysosome mitochondria apoptosis Sf9 cells Cry1Ab oligomer formation Sf21 cell line Ostrinia nubilalis Lobesia botrana Leptinotarsa decemlineata bioassay Cyt2Aa2 toxin protein-lipid binding erythrocyte membrane AFM QCM-D Asian corn borer ABCC2 CRISPR/Cas9 Cry1Fa resistance chitin-binding protein adhesion peritrophic matrix Vip3A Spodoptera litura site-directed mutagenesis Cry Cyt parasporins S-layer proteins Vip Sip membrane receptors insecticidal activity anticancer activity Aedes aegypti minor proteins synergy mosquito control Bti Spodoptera frugiperda cadherin mode of action of Cry toxin insecticidal proteins insect resistance tobacco budworm Bacillus thuringiensis proteins coleopteran pests structure mode of action 3D-structure biological control antimicrobial peptide gut microbiota vegetative insecticidal proteins pyramids 3D-Cry toxins in vitro evolution rational design toxin enhancement n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general |
| topic_facet | Bacillus thuringiensis Plutella xylostella Cry1Ac resistance trypsin-like midgut protease protoxin activation Spodoptera spp., Helicoverpa armigera Mamestra brassicae Anticarsia gemmatalis Ostrinia furnacalis Cry2Ab toxin Bombyx mori ATP-binding cassette subfamily a member 2 (ABCA2) genome editing transcription activator-like effector-nucleases (TALENs) HEK293T cell functional receptor Vip3Aa lysosome mitochondria apoptosis Sf9 cells Cry1Ab oligomer formation Sf21 cell line Ostrinia nubilalis Lobesia botrana Leptinotarsa decemlineata bioassay Cyt2Aa2 toxin protein-lipid binding erythrocyte membrane AFM QCM-D Asian corn borer ABCC2 CRISPR/Cas9 Cry1Fa resistance chitin-binding protein adhesion peritrophic matrix Vip3A Spodoptera litura site-directed mutagenesis Cry Cyt parasporins S-layer proteins Vip Sip membrane receptors insecticidal activity anticancer activity Aedes aegypti minor proteins synergy mosquito control Bti Spodoptera frugiperda cadherin mode of action of Cry toxin insecticidal proteins insect resistance tobacco budworm Bacillus thuringiensis proteins coleopteran pests structure mode of action 3D-structure biological control antimicrobial peptide gut microbiota vegetative insecticidal proteins pyramids 3D-Cry toxins in vitro evolution rational design toxin enhancement n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general |
| url | ONIX_20220111_9783036520490_851 |