Expression of recombinant and mosaic Cry1Ac receptors from Helicoverpa armigera and their influences on the cytotoxicity of activated Cry1Ac to ... View Full Text


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Article Info

DATE

2014-11-21

AUTHORS

Peng Xu, Mayira Islam, Yutao Xiao, Fei He, Yi Li, Jianxin Peng, Huazhu Hong, Chenxi Liu, Kaiyu Liu

ABSTRACT

Bacillus thuringiensis (Bt) toxin receptors play important roles in the killing of pests, and investigation on characterization of the receptors is essential for utilization of Bt and management of insect resistance. Here, recombinant and mosaic receptors of Bt Cry1Ac toxin from Helicoverpa armigera were expressed in Spodoptera litura Sl-HP cells and their influences on cytotoxicity of activated Cry1Ac toxin were investigated. When H. armigera aminopeptidase N1 (APN1), alkaline phosphatase 2 (ALP2) and cadherin fused with or without GFP tag were, respectively, expressed in Sl-HP cells, live cell-immunofluorescence staining detection revealed that the quantity of the toxin binding to cadherin or cadherin-GFP was much more than that binding to ALP2 and APN1 or their fusion proteins with GFP, and only the cadherin- or cadherin-GFP-expressing cells showed aberrant cell morphology after the treatment of the toxin at low concentrations. ALP2 and APN1 fused with or without GFP tag did not significantly enhance the cadherin-mediated cytotoxicity of the toxin. The mosaic ALP-TBR-GFP-GPI was located on cell membrane, but did not bind to the toxin. The mosaic truncated cadherin-GFP-GPI was not located on cell membrane even if the signal peptide was sustained. The concentrations of the toxin resulting in swelling of 50 % cells for noncadherin-expressing Sl-HP cells and cadherin-expressing Hi5 cells were 5.08 and 9.50 µg/ml within 1 h, respectively. Taken together, our data have indicated that the binding affinity of ALP2 and APN1 to activated Cry1Ac toxin is much weaker than that of cadherin and both ALP2 and APN1 do not enhance the cytotoxicity of the toxin even though cadherin is co-expressed, and the mosaic receptor of ALP2 inserted with cadherin toxin binding domain does not mediate cytotoxicity of the toxin. In addition, the noncadherin-expressing Sl-HP cells are more susceptible to activated Cry1Ac than the cadherin-expressing Hi5 cells. More... »

PAGES

481-496

References to SciGraph publications

  • 2005-05-27. Cytotoxicity of Bacillus thuringiensis Cry1Ab toxin depends on specific binding of the toxin to the cadherin receptor BT-R1 expressed in insect cells in CELL DEATH & DIFFERENTIATION
  • 2012-06-13. Widespread adoption of Bt cotton and insecticide decrease promotes biocontrol services in NATURE
  • 2006. BACILLUS THURINGIENSIS INSECTICIDAL CRY1AB TOXIN DOES NOT AFFECT THE MEMBRANE INTEGRITY OF THE MAMMALIAN INTESTINAL EPITHELIAL CELLS: AN IN VITRO STUDY in IN VITRO CELLULAR & DEVELOPMENTAL BIOLOGY - ANIMAL
  • 2005-07. Gene cloning and expression of cadherin in midgut of Helicoverpa armigera and its Cry1A binding region in SCIENCE CHINA LIFE SCIENCES
  • 2008-07. Highly passage of Spodoptera litura cell line causes its permissiveness to baculovirus infection in CYTOTECHNOLOGY
  • 2009-01-13. Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells? in CELLULAR AND MOLECULAR LIFE SCIENCES
  • 2001-10. Aminopeptidase-N from the Helicoverpa armigera (Hubner) Brush Border Membrane Vesicles as a Receptor of Bacillus thuringiensis Cry1Ac δ-Endotoxin in CURRENT MICROBIOLOGY
  • 2006-01. Bacillus thuringiensis insecticidal crylab toxin does not affect the membrane integrity of the mammalian intestinal epithelial cells: An in vitro study in IN VITRO CELLULAR & DEVELOPMENTAL BIOLOGY - ANIMAL
  • 2005-10-25. Purification and Characterization of Cry1Ac Toxin Binding Proteins from the Brush Border Membrane of Helicoverpa armigera Midgut in CURRENT MICROBIOLOGY
  • 2011-06-10. Role of alkaline phosphatase in insecticidal action of Cry1Ac against Helicoverpa armigera larvae in BIOTECHNOLOGY LETTERS
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    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/25412589


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