Molecular characterization of two acetylcholinesterase genes from the brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae)

详细信息	查看全文 | 推荐本文 |

• 作者：Bao-Ling Li^a ; Wei Chen^a ; Li Liu^b ; Xue-Chao Zhang^a ; Yan-Yuan Bao^a ; Jia-An Cheng^a ; Zeng-Rong Zhu^a ; ^{zrzhu@zju.edu.cn} ; Chuan-Xi Zhang^a ; ^{chxzhang@zju.edu.cn}
• 关键词：Nilaparvata lugens ; Acetylcholinesterase ; NlAChE1 ; NlAChE2 ; Transcription
• 刊名：Pesticide Biochemistry and Physiology
• 出版年：2012
• 期刊代码：182_00483575
• 类别：bio
• 出版时间：March, 2012
• 卷：102
• 期：3
• 页码：198-203
• 文件大小：1157 K

摘要

Acetylcholinesterase (AChE), which is encoded by the <em>aceem> gene, catalyzes the hydrolysis of the neurotransmitter acetylcholine to terminate nerve impulses at the postsynaptic membrane. AChE is a primary target of many insecticides including organophosphates (OP) and carbamates (CB). In this study, full-length cDNA sequences of two <em>aceem> genes (<em>Nlace1em> and <em>Nlace2em>) were sequenced from the brown planthopper (BPH) <em>Nilaparvata lugensem>, the most destructive insect pest of rice crops. <em>Nlace1em> cDNA is 2842 nucleotides long and contains an ORF potentially encoding a 790 amino acid peptide. <em>Nlace2em> cDNA is 2852 bp in length and contains an ORF that potentially encodes a 672 amino acid peptide. NlAChE1 has an identity of 40%with NlAChE2 at the amino acid sequence level. Phylogenetic analysis of 59 AChEs from 32 animal species showed that NlAChE1 is most closely related to AChE1s from <em>Blattella germanicaem> and <em>Nephotettix cincticepsem>, while NlAChE2 is most closely related to AChE2 from <em>N. cincticepsem>. Quantitative RT-PCR analysis showed that <em>Nlace1em> is expressed at a much higher level than <em>Nlace2em> in all developmental stages and tissues, demonstrating that NlAChE1 may be the dominant AChE form of the two enzymes. This result will help reveal the resistance mechanism of <em>N. lugensem> to organophosphorous and carbamate insecticides and promote development of more selective insecticides targeting the main NlAChE1.