Characterization and functional analysis of beta-1,3-galactosyltransferase involved in Cry1Ac resistance from Helicoverpa armigera (Hubner)

文献类型： 外文期刊

第一作者： Gao Xi-wu

作者： Gao Xi-wu;Zhang Li-li;Liang Ge-mei;Cao Guang-chun;Guo Yu-yuan

作者机构：

关键词： beta-1,3-galactosyltransferase;Cry1Ac;resistance;Helicoverpa armigera;RNAi

期刊名称：JOURNAL OF INTEGRATIVE AGRICULTURE （ 影响因子：2.848； 五年影响因子：2.979 ）

ISSN： 2095-3119

年卷期： 2015 年 14 卷 2 期

页码：

收录情况： SCI

摘要： Carbohydrate chains are the principal antigens by which Bacillus thuringiensis (Bt) identify receptor proteins. The interaction between the antigen and Bt causes a pore in the membrane of midgut epithelial cells of insects. Receptor proteins, such as aminopeptidase N and alkaline phosphatase, are glycoproteins. Cadherin is another cell surface receptor protein which has potential glycosylation sites. Glycosyltransferase is very important for the synthesis and modification of receptor proteins. It can indirectly influence the function of Bt. The 1 950 bp full-length cDNA encoding beta-1,3-galactosyltransferase was cloned from the the midgut of Helicoverpa armigera by degenerative PCR combined with RACE techniques (GAL-Harm, GenBank accession no.: GQ904195.1) with two potential N-glycosylation sites ((NNTI160)-N-157 and (NKTL275)-N-272). Protein sequence alignments revealed that H. armigera beta-1,3-galactosyltransferase shared high identity with beta-1,3-galactosyltransferase in other insect species. The expression level of the beta-1,3-galactosyltransferase gene in Cry1Ac-resistant H. armigera larvae was 9.2-fold higher than that in susceptible strain. The function of beta-1,3-galactosyltransferase was investigated using RNAi technique. The result showed Cry1Ac enhanced the toxicity against the siRNA-treated larvae compared with non-siRNA-treated ones, which indicated beta-1,3-galactosyltransferase played an important role for the insecticidal toxicity of Cry1Ac in H. armigera.

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