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dc.contributor.editorBel, Yolanda
dc.contributor.editorFerré, Juan
dc.contributor.editorHernández-Martínez, Patricia
dc.date.accessioned2022-01-11T13:49:29Z
dc.date.available2022-01-11T13:49:29Z
dc.date.issued2021
dc.identifierONIX_20220111_9783036520490_851
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/77019
dc.description.abstractBacillus 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.
dc.languageEnglish
dc.subject.classificationthema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: generalen_US
dc.subject.otherBacillus thuringiensis
dc.subject.otherPlutella xylostella
dc.subject.otherCry1Ac resistance
dc.subject.othertrypsin-like midgut protease
dc.subject.otherprotoxin activation
dc.subject.otherSpodoptera spp., Helicoverpa armigera
dc.subject.otherMamestra brassicae
dc.subject.otherAnticarsia gemmatalis
dc.subject.otherOstrinia furnacalis
dc.subject.otherCry2Ab toxin
dc.subject.otherBombyx mori
dc.subject.otherATP-binding cassette subfamily a member 2 (ABCA2)
dc.subject.othergenome editing
dc.subject.othertranscription activator-like effector-nucleases (TALENs)
dc.subject.otherHEK293T cell
dc.subject.otherfunctional receptor
dc.subject.otherVip3Aa
dc.subject.otherlysosome
dc.subject.othermitochondria
dc.subject.otherapoptosis
dc.subject.otherSf9 cells
dc.subject.otherCry1Ab
dc.subject.otheroligomer formation
dc.subject.otherSf21 cell line
dc.subject.otherOstrinia nubilalis
dc.subject.otherLobesia botrana
dc.subject.otherLeptinotarsa decemlineata
dc.subject.otherbioassay
dc.subject.otherCyt2Aa2 toxin
dc.subject.otherprotein-lipid binding
dc.subject.othererythrocyte membrane
dc.subject.otherAFM
dc.subject.otherQCM-D
dc.subject.otherAsian corn borer
dc.subject.otherABCC2
dc.subject.otherCRISPR/Cas9
dc.subject.otherCry1Fa
dc.subject.otherresistance
dc.subject.otherchitin-binding protein
dc.subject.otheradhesion
dc.subject.otherperitrophic matrix
dc.subject.otherVip3A
dc.subject.otherSpodoptera litura
dc.subject.othersite-directed mutagenesis
dc.subject.otherCry
dc.subject.otherCyt
dc.subject.otherparasporins
dc.subject.otherS-layer proteins
dc.subject.otherVip
dc.subject.otherSip
dc.subject.othermembrane receptors
dc.subject.otherinsecticidal activity
dc.subject.otheranticancer activity
dc.subject.otherAedes aegypti
dc.subject.otherminor proteins
dc.subject.othersynergy
dc.subject.othermosquito control
dc.subject.otherBti
dc.subject.otherSpodoptera frugiperda
dc.subject.othercadherin
dc.subject.othermode of action of Cry toxin
dc.subject.otherinsecticidal proteins
dc.subject.otherinsect resistance
dc.subject.othertobacco budworm
dc.subject.otherBacillus thuringiensis proteins
dc.subject.othercoleopteran pests
dc.subject.otherstructure
dc.subject.othermode of action
dc.subject.other3D-structure
dc.subject.otherbiological control
dc.subject.otherantimicrobial peptide
dc.subject.othergut microbiota
dc.subject.othervegetative insecticidal proteins
dc.subject.otherpyramids
dc.subject.other3D-Cry toxins
dc.subject.otherin vitro evolution
dc.subject.otherrational design
dc.subject.othertoxin enhancement
dc.subject.othern/a
dc.titleBacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-2050-6
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036520490
oapen.relation.isbn9783036520506
oapen.pages340
oapen.place.publicationBasel, Switzerland


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