title: Identification of ABCC2 as a binding protein of Cry1Ac on brush border membrane vesicles from Helicoverpa armigera by an improved pull-down assay.
abstract: Cry1Ac toxin-binding proteins from Helicoverpa armigera brush border membrane vesicles were identified by an improved pull-down method that involves coupling Cry1Ac to CNBr agarose combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS). According to the LC-MS/MS results, Cry1Ac toxin could bind to six classes of aminopeptidase-N, alkaline phosphatase, cadherin-like protein, ATP-binding cassette transporter subfamily C protein (ABCC2), actin, ATPase, polycalin, and some other proteins not previously characterized as Cry toxin-binding molecules such as dipeptidyl peptidase or carboxyl/choline esterase and some serine proteases. This is the first report that suggests the direct binding of Cry1Ac toxin to ABCC2 in H. armigera.
authors.affiliation: State Key Laboratory of Rice Biology, Institute of Biotechnology, Zhejiang University, No. 866 Yuhangtang Road, Xihu District, Hangzhou, 310012, China.|State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Zishan
authors.initials: Z
authors.lastname: Zhou
authors.affiliation: State Key Laboratory of Rice Biology, Institute of Biotechnology, Zhejiang University, No. 866 Yuhangtang Road, Xihu District, Hangzhou, 310012, China.
authors.forename: Zeyu
authors.initials: Z
authors.lastname: Wang
authors.affiliation: State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Yuxiao
authors.initials: Y
authors.lastname: Liu
authors.affiliation: State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Gemei
authors.initials: G
authors.lastname: Liang
authors.affiliation: State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Changlong
authors.initials: C
authors.lastname: Shu
authors.affiliation: State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Fuping
authors.initials: F
authors.lastname: Song
authors.affiliation: State Key Laboratory of Rice Biology, Institute of Biotechnology, Zhejiang University, No. 866 Yuhangtang Road, Xihu District, Hangzhou, 310012, China.|State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Xueping
authors.initials: X
authors.lastname: Zhou
authors.affiliation: Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Apdo. Postal 510-3, Morelos, 62250, Mexico.
authors.forename: Alejandra
authors.initials: A
authors.lastname: Bravo
authors.affiliation: Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Apdo. Postal 510-3, Morelos, 62250, Mexico.
authors.forename: Mario
authors.initials: M
authors.lastname: Soberón
authors.affiliation: State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 Yuanmingyuan West Road, Haidian District, Beijing, 100193, China.
authors.forename: Jie
authors.initials: J
authors.lastname: Zhang
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D001413:Bacillus thuringiensis / Q000378:metabolism*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism*; D002853:Chromatography, Liquid; D004731:Endotoxins / Q000378:metabolism*; D006460:Hemolysin Proteins / Q000378:metabolism*; D009036:Moths / Q000382:microbiology*; D000089762:Multidrug Resistance-Associated Protein 2; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000378:metabolism*; D011485:Protein Binding; D053719:Tandem Mass Spectrometry
chemical_list: D000251:Adenosine Triphosphatases; D000469:Alkaline Phosphatase; D000626:Aminopeptidases; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; D000089762:Multidrug Resistance-Associated Protein 2; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis
keywords: ABCC2; Bacillus thuringiensis; Cry1Ac; Helicoverpa armigera.; alkaline phosphatase; aminopeptidase-N; cadherin