ATP Synthase Subunit α from Helicoverpa armigera Acts as a Receptor of Bacillus thuringiensis Cry1Ac and Synergizes Cry1Ac Toxicity.
Sign Up to like & getrecommendations! Published in 2023 at "Journal of agricultural and food chemistry"
DOI: 10.1021/acs.jafc.3c00259
Abstract: Insect resistance to Bacillus thuringiensis (Bt) toxins has led to an urgent need to explore the insecticidal mechanisms of Bt. Previous studies indicated that Helicoverpa armigera ATP synthase subunit α (HaATPs-α) is involved in Cry1Ac… read more here.
Keywords: bacillus thuringiensis; cry1ac toxicity; cry1ac; haatps ... See more keywords
Aminopeptidase N1 is involved in Bacillus thuringiensis Cry1Ac toxicity in the beet armyworm, Spodoptera exigua
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DOI: 10.1038/srep45007
Abstract: Understanding how insecticidal proteins from the bacterium Bacillus thuringiensis (Bt) interact with their hosts is crucial to fully explain the molecular bases of Bt specificity and insecticidal activity. Previous studies support ATP binding cassette transporters… read more here.
Keywords: cry1ac toxicity; armyworm spodoptera; cry1ac; spodoptera exigua ... See more keywords
The Cadherin Cry1Ac Binding-Region is Necessary for the Cooperative Effect with ABCC2 Transporter Enhancing Insecticidal Activity of Bacillus thuringiensis Cry1Ac Toxin
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DOI: 10.3390/toxins11090538
Abstract: Bacillus thuringiensis Cry1Ac toxin binds to midgut proteins, as cadherin (CAD) and ABCC2 transporter, to form pores leading to larval death. In cell lines, co-expression of CAD and ABCC2 enhance Cry1Ac toxicity significantly, but the… read more here.
Keywords: abcc2; cry1ac toxicity; gfp; cry1ac ... See more keywords