Identification of ABCC2 as a binding protein of Cry1Ac on brush border membrane vesicles from Helicoverpa armigera by an improved pull‐down assay. Issue 4 (1st April 2016)

• Record Type: Journal Article
• Authors: Zhou, Zishan; Wang, Zeyu; Liu, Yuxiao; Liang, Gemei; Shu, Changlong; Song, Fuping; Zhou, Xueping; Bravo, Alejandra; Soberón, Mario; Zhang, Jie
• Is Part Of: MicrobiologyOpen. Volume 5:Issue 4(2016:Aug.)
• Page Start: 659
• Page End: 669
• Publication Date: 2016-04-01
• Subjects: ABCC2 -- alkaline phosphatase -- aminopeptidase‐N -- Bacillus thuringiensis -- cadherin -- Cry1Ac -- Helicoverpa armigera.; Microbiology -- Periodicals; 579
• DOI: 10.1002/mbo3.360
• Languages: English
• ISSNs: 2045-8827

Abstract

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 . Abstract : Cry1Ac toxin could bound to six classes of aminopeptidase‐N, alkaline phosphatase, cadherin‐like 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 provides evidence of direct binding of Cry1Ac toxin to ABCC2 in Helicoverpa armigera .