文献类型：期刊文献

英文题名：Bacillus thuringiensis Cry3Aa fused to a cellulase-binding peptide shows increased toxicity against the longhorned beetle

作者：Guo, Chang-Hua[1,2] Zhao, Shu-Tang[2,3] Ma, Yuan[2] Hu, Jian-Jun[2,3] Han, Xiao-Jiao[1,2] Chen, Jun[2,3] Lu, Meng-Zhu[2,3]

第一作者：Guo, Chang-Hua

通信作者：Lu, M.-Z.

机构：[1] International Centre for Bamboo and Rattan, Beijing 100102, China; [2] State Key Laboratory of Tree Genetics and Breeding, Chinese Academy of Forestry, Beijing 100091, China; [3] Research Institute of Forestry, Chinese Academy of Forestry, Beijing 100091, China

年份：2012

卷号：93

期号：3

起止页码：1249-1256

外文期刊名：Applied Microbiology and Biotechnology

收录：EI(收录号：20120514737209);Scopus(收录号：2-s2.0-84856378412)

语种：英文

外文关键词：Toxic materials - Bioassay - Bacteriology

摘要：Cry3 class toxins are used extensively for biological control of coleopteran larvae. We previously identified a peptide (PCx) from a phage display library that specifically binds Cx-cellulase from the midgut of Anoplophora glabripennis Motschulsky (Asian longhorn beetle) larvae. Here, we added a DNA fragment that encodes the peptide onto either end of the cry3Aa gene and tested the expressed PCx-Cry3Aa and Cry3Aa-PCx proteins for insecticidal activity in the longhorned beetle. An insect bioassay revealed that, compared with native Cry3Aa, the two modified Cry3Aa proteins had significantly higher lethality, with PCx-Cry3Aa exhibiting a mortality rate almost three times that of Cry3Aa. We also proposed that the increased lethality in larvae fed with PCx-Cry3Aa or Cry3Aa-PCx would be attributable to the binding of the toxin with Cx-cellulase, thereby increasing toxin retention in the midgut. The significantly enhanced insecticidal activity of Cry3Aa fused with the Cx-cellulase binding peptide provides a new strategy for increasing toxin efficacy against the longhorned beetle. These uniquely modified Cry3Aa proteins have potential use for pest control. ? 2011 Springer-Verlag.