05267nam 2201321z- 450 991055764610332120240411214232.0(CKB)5400000000044992(oapen)https://directory.doabooks.org/handle/20.500.12854/77019(EXLCZ)99540000000004499220202201d2021 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierBacillus thuringiensis Toxins: Functional Characterization and Mechanism of ActionBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20211 electronic 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 & information: generalbicsscBacillus thuringiensisPlutella xylostellaCry1Ac resistancetrypsin-like midgut proteaseprotoxin activationSpodoptera spp., Helicoverpa armigeraMamestra brassicaeAnticarsia gemmatalisOstrinia furnacalisCry2Ab toxinBombyx moriATP-binding cassette subfamily a member 2 (ABCA2)genome editingtranscription activator-like effector-nucleases (TALENs)HEK293T cellfunctional receptorVip3AalysosomemitochondriaapoptosisSf9 cellsCry1Aboligomer formationSf21 cell lineOstrinia nubilalisLobesia botranaLeptinotarsa decemlineatabioassayCyt2Aa2 toxinprotein-lipid bindingerythrocyte membraneAFMQCM-DAsian corn borerABCC2CRISPR/Cas9Cry1Faresistancechitin-binding proteinadhesionperitrophic matrixVip3ASpodoptera liturasite-directed mutagenesisCryCytparasporinsS-layer proteinsVipSipmembrane receptorsinsecticidal activityanticancer activityAedes aegyptiminor proteinssynergymosquito controlBtiSpodoptera frugiperdacadherinmode of action of Cry toxininsecticidal proteinsinsect resistancetobacco budwormBacillus thuringiensis proteinscoleopteran pestsstructuremode of action3D-structurebiological controlantimicrobial peptidegut microbiotavegetative insecticidal proteinspyramids3D-Cry toxinsin vitro evolutionrational designtoxin enhancementResearch & information: generalBel Yolandaedt1313328Ferré JuanedtHernández-Martínez PatriciaedtBel YolandaothFerré JuanothHernández-Martínez PatriciaothBOOK9910557646103321Bacillus thuringiensis Toxins: Functional Characterization and Mechanism of Action3031291UNINA