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The Journal of biological chemistry v.292 no.7, 2017년, pp.2933 - 2943   SCI SCIE
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A Single Point Mutation Resulting in Cadherin Mislocalization Underpins Resistance against Bacillus thuringiensis Toxin in Cotton Bollworm

Xiao, Yutao (From the State Key Laboratory for Biology of Plant Disease and Insect Pests, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing 100193, China, ) ; Dai, Qing (the College of Life Science, Central China Normal University, No. 152 Luoyu Avenue, Wuhan 430079, China, and ) ; Hu, Ruqin (From the State Key Laboratory for Biology of Plant Disease and Insect Pests, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing 100193, China, ) ; Pacheco, Sabino (the Instituto de Biotecnologóía, Universidad Nacional Autóíónoma de Móíóéxico, Apdo. Postal 510-3, Cuernavaca 62250, Morelos, Mexico ) ; Yang, Yongbo (the College of Life Science, Central China Normal University, No. 152 Luoyu Avenue, Wuhan 430079, China, and ) ; Liang, Gemei (From the State Key Laboratory for Biology of Plant Disease and Insect Pests, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing 100193, China, ) ; Soberón, Mario (the Instituto de Biotecnologóía, Universidad Nacional Auto ) ; Bravo, Alejandra ; Liu, Kaiyu ; Wu, Kongming ;
  • 초록  

    Transgenic plants that produce Bacillus thuringiensis (Bt) crystalline (Cry) toxins are cultivated worldwide to control insect pests. Resistance to B. thuringiensis toxins threatens this technology, and although different resistance mechanisms have been identified, some have not been completely elucidated. To gain new insights into these mechanisms, we performed multiple back-crossing from a 3000-fold Cry1Ac-resistant BtR strain from cotton bollworm ( Helicoverpa armigera ), isolating a 516-fold Cry1Ac-resistant strain (96CAD). Cry1Ac resistance in 96CAD was tightly linked to a mutant cadherin allele (mHaCad) that contained 35 amino acid substitutions compared with HaCad from a susceptible strain (96S). We observed significantly reduced levels of the mHaCad protein on the surface of the midgut epithelium in 96CAD as compared with 96S. Expression of both cadherin alleles from 96CAD and 96S in insect cells and immunofluorescence localization in insect midgut tissue sections showed that the HaCAD protein from 96S localizes on the cell membrane, whereas the mutant 96CAD-mHaCad was retained in the endoplasmic reticulum (ER). Mapping of the mutations identified a D172G substitution mainly responsible for cadherin mislocalization. Our finding of a mutation affecting membrane receptor trafficking represents an unusual and previously unrecognized B. thuringiensis resistance mechanism.


  • 주제어

    antibiotic resistance .   bacterial toxin .   insect .   mutant .   plasma membrane .   receptor modification .   Bacillus thuringiensis .   Cry1Ac .   Helicoverpa armigera .   receptor trafficking.  

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