Yakun Zhang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Yakun Zhang has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Dan Zhao
College of Plant Protection, Hebei Agricultural University, Baoding 071000, China
1 shared publication - Wei Guo
Plant Science and Technology College, Beijing University of Agriculture, Beijing 102206, China
1 shared publication - Wei Wang
College of Plant Protection, Hebei Agricultural University, Baoding 071000, China
1 shared publication - Xiaoping Yan
College of Plant Protection, Hebei Agricultural University, Baoding 071000, China
1 shared publication - Xiaoyun Wang
Key Laboratory of Crop Pests in Northern Cold Regions of Heilongjiang Province, College of Plant Protection, Northeast Agricultural University, No. 600 Changjiang Road, Xiangfang District, Harbin 150030, China
1 shared publication - Yajun Bao
College of Plant Protection, Hebei Agricultural University, Baoding 071000, China
1 shared publication
Latest Publications
- Open Access
- 30 November 2017
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 18 (12) , 2575
Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin
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.
- 30 November 2017
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 18 (12) , 2575
Open AccessIdentification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin
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.