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Open AccessArticle

Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin

by Yakun Zhang 1,†, Dan Zhao 1,†, Xiaoping Yan 1, Wei Guo 1,2,*, Yajun Bao 1, Wei Wang 1 and Xiaoyun Wang 3
1
College of Plant Protection, Hebei Agricultural University, Baoding 071000, China
2
Plant Science and Technology College, Beijing University of Agriculture, Beijing 102206, China
3
College of Agriculture, Northeast Agricultural University, Harbin 150038, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2017, 18(12), 2575; https://doi.org/10.3390/ijms18122575
Received: 26 October 2017 / Revised: 21 November 2017 / Accepted: 22 November 2017 / Published: 30 November 2017
(This article belongs to the Special Issue Molecular Entomology of Insects of Economic Importance)
The fall webworm, Hyphantria cunea (Drury) is a major invasive pest in China. Aminopeptidase N (APN) isoforms in lepidopteran larvae midguts are known for their involvement in the mode of action of insecticidal crystal (Cry) proteins from Bacillus thuringiensis. In the present work, we identified a putative Cry1Ab toxin-binding protein, an APN isoform designated HcAPN3, in the midgut of H. cunea by ligand blot and mass spectrometry. HcAPN3 was highly expressed throughout all larval developmental stages and was abundant in the midgut and hindgut tissues. HcAPN3 was down-regulated at 6 h, then was up-regulated significantly at 12 h and 24 h after Cry1Ab toxin treatment. We expressed HcAPN3 in insect cells and detected its interaction with Cry1Ab toxin by ligand blot assays. Furthermore, RNA interference (RNAi) against HcAPN3 using oral delivery and injection of double-stranded RNA (dsRNA) resulted in a 61–66% decrease in transcript level. Down-regulating of the expression of HcAPN3 was closely associated with reduced susceptibility of H. cunea to Cry1Ab. In addition, the HcAPN3E fragment peptide expressed in Escherichia coli enhanced Cry1Ab toxicity against H. cunea larvae. This work represents the first evidence to suggest that an APN in H. cunea is a putative binding protein involved in Cry1Ab susceptibility. View Full-Text
Keywords: Hyphantria cunea; HcAPN3; Cry1Ab; binding protein; RNAi Hyphantria cunea; HcAPN3; Cry1Ab; binding protein; RNAi
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Zhang, Y.; Zhao, D.; Yan, X.; Guo, W.; Bao, Y.; Wang, W.; Wang, X. Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin. Int. J. Mol. Sci. 2017, 18, 2575.

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