05312nam 2201345z- 450 991055764610332120220111(CKB)5400000000044992(oapen)https://directory.doabooks.org/handle/20.500.12854/77019(oapen)doab77019(EXLCZ)99540000000004499220202201d2021 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierBacillus thuringiensis Toxins: Functional Characterization and Mechanism of ActionBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20211 online resource (340 p.)3-0365-2049-X 3-0365-2050-3 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.Bacillus thuringiensis ToxinsResearch and information: generalbicssc3D-Cry toxins3D-structureABCC2adhesionAedes aegyptiAFManticancer activityAnticarsia gemmatalisantimicrobial peptideapoptosisAsian corn borerATP-binding cassette subfamily a member 2 (ABCA2)Bacillus thuringiensisBacillus thuringiensis proteinsbioassaybiological controlBombyx moriBticadherinchitin-binding proteincoleopteran pestsCRISPR/Cas9CryCry1AbCry1Ac resistanceCry1FaCry2Ab toxinCytCyt2Aa2 toxinerythrocyte membranefunctional receptorgenome editinggut microbiotaHEK293T cellin vitro evolutioninsect resistanceinsecticidal activityinsecticidal proteinsLeptinotarsa decemlineataLobesia botranalysosomeMamestra brassicaemembrane receptorsminor proteinsmitochondriamode of actionmode of action of Cry toxinmosquito controln/aoligomer formationOstrinia furnacalisOstrinia nubilalisparasporinsperitrophic matrixPlutella xylostellaprotein-lipid bindingprotoxin activationpyramidsQCM-Drational designresistanceS-layer proteinsSf21 cell lineSf9 cellsSipsite-directed mutagenesisSpodoptera frugiperdaSpodoptera lituraSpodoptera spp., Helicoverpa armigerastructuresynergytobacco budwormtoxin enhancementtranscription activator-like effector-nucleases (TALENs)trypsin-like midgut proteasevegetative insecticidal proteinsVipVip3AVip3AaResearch and information: generalBel Yolandaedt1313328Ferré JuanedtHernández-Martínez PatriciaedtBel YolandaothFerré JuanothHernández-Martínez PatriciaothBOOK9910557646103321Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action3031291UNINA