<em>Bacillus thuringiensis</em> 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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Other Authors: Bel, Yolanda (Editor), Ferré, Juan (Editor), Hernández-Martínez, Patricia (Editor)
Format: Book Chapter
Published: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021
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Online Access:Get Fullteks
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020 |a books978-3-0365-2050-6 
020 |a 9783036520490 
020 |a 9783036520506 
024 7 |a 10.3390/books978-3-0365-2050-6  |c doi 
041 0 |a English 
042 |a dc 
072 7 |a GP  |2 bicssc 
100 1 |a Bel, Yolanda  |4 edt 
700 1 |a Ferré, Juan  |4 edt 
700 1 |a Hernández-Martínez, Patricia  |4 edt 
700 1 |a Bel, Yolanda  |4 oth 
700 1 |a Ferré, Juan  |4 oth 
700 1 |a Hernández-Martínez, Patricia  |4 oth 
245 1 0 |a <em>Bacillus thuringiensis</em> Toxins: Functional Characterization and Mechanism of Action 
260 |a Basel, Switzerland  |b MDPI - Multidisciplinary Digital Publishing Institute  |c 2021 
300 |a 1 electronic resource (340 p.) 
506 0 |a Open Access  |2 star  |f Unrestricted online access 
520 |a 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. 
540 |a Creative Commons  |f https://creativecommons.org/licenses/by/4.0/  |2 cc  |4 https://creativecommons.org/licenses/by/4.0/ 
546 |a English 
650 7 |a Research & information: general  |2 bicssc 
653 |a Bacillus thuringiensis 
653 |a Plutella xylostella 
653 |a Cry1Ac resistance 
653 |a trypsin-like midgut protease 
653 |a protoxin activation 
653 |a Spodoptera spp., Helicoverpa armigera 
653 |a Mamestra brassicae 
653 |a Anticarsia gemmatalis 
653 |a Ostrinia furnacalis 
653 |a Cry2Ab toxin 
653 |a Bombyx mori 
653 |a ATP-binding cassette subfamily a member 2 (ABCA2) 
653 |a genome editing 
653 |a transcription activator-like effector-nucleases (TALENs) 
653 |a HEK293T cell 
653 |a functional receptor 
653 |a Vip3Aa 
653 |a lysosome 
653 |a mitochondria 
653 |a apoptosis 
653 |a Sf9 cells 
653 |a Cry1Ab 
653 |a oligomer formation 
653 |a Sf21 cell line 
653 |a Ostrinia nubilalis 
653 |a Lobesia botrana 
653 |a Leptinotarsa decemlineata 
653 |a bioassay 
653 |a Cyt2Aa2 toxin 
653 |a protein-lipid binding 
653 |a erythrocyte membrane 
653 |a AFM 
653 |a QCM-D 
653 |a Asian corn borer 
653 |a ABCC2 
653 |a CRISPR/Cas9 
653 |a Cry1Fa 
653 |a resistance 
653 |a chitin-binding protein 
653 |a adhesion 
653 |a peritrophic matrix 
653 |a Vip3A 
653 |a Spodoptera litura 
653 |a site-directed mutagenesis 
653 |a Cry 
653 |a Cyt 
653 |a parasporins 
653 |a S-layer proteins 
653 |a Vip 
653 |a Sip 
653 |a membrane receptors 
653 |a insecticidal activity 
653 |a anticancer activity 
653 |a Aedes aegypti 
653 |a minor proteins 
653 |a synergy 
653 |a mosquito control 
653 |a Bti 
653 |a Spodoptera frugiperda 
653 |a cadherin 
653 |a mode of action of Cry toxin 
653 |a insecticidal proteins 
653 |a insect resistance 
653 |a tobacco budworm 
653 |a Bacillus thuringiensis proteins 
653 |a coleopteran pests 
653 |a structure 
653 |a mode of action 
653 |a 3D-structure 
653 |a biological control 
653 |a antimicrobial peptide 
653 |a gut microbiota 
653 |a vegetative insecticidal proteins 
653 |a pyramids 
653 |a 3D-Cry toxins 
653 |a in vitro evolution 
653 |a rational design 
653 |a toxin enhancement 
653 |a n/a 
856 4 0 |a www.oapen.org  |u https://mdpi.com/books/pdfview/book/4629  |7 0  |z Get Fullteks 
856 4 0 |a www.oapen.org  |u https://directory.doabooks.org/handle/20.500.12854/77019  |7 0  |z DOAB: description of the publication