Mutation in PgABCC2 confers low-level resistance to Cry1Ac in pink bollworm

文献类型： 外文期刊

第一作者： Wang, Ling

作者： Wang, Ling;Xu, Dong;Cong, Shengbo;Wan, Peng;Xu, Min;He, Lu;Liu, Kaiyu;Wei, Wei;Wan, Peng

作者机构：

关键词： Bacillus thuringiensis; pink bollworm; Cry1Ac; ABCC2; resistance mechanism

期刊名称：PEST MANAGEMENT SCIENCE （ 影响因子：4.1； 五年影响因子：4.4 ）

ISSN： 1526-498X

年卷期： 2024 年

页码：

收录情况： SCI

摘要： BACKGROUND: With the increasing incidence of pest resistance to transgenic crops producing Bacillus thuringiensis (Bt) proteins in the field, elucidating the molecular basis of resistance is important for monitoring, delaying and countering pest resistance. Previous work revealed that mutation or down-regulated expression of the cadherin gene (PgCad1) is associated with pink bollworm (Pectinophora gossypiella) resistance to Cry1Ac, and 20 mutant PgCad1 alleles (r1-r20) were characterized. Here, we tested the hypothesis that the ABC transporter PgABCC2 is a functional receptor for the Bt toxin Cry1Ac and that a mutation is associated with resistance. RESULTS: We identified and characterized the first resistance allele (r(C2)) of PgABCC2 in the laboratory-selected Cry1Ac-resistant strain AQ-C2 of pink bollworm. The r(C2) allele had a one-base deletion in exon20, resulting in a frameshift and the introduction of a premature stop codon. This resulting PgABCC2 protein had a truncated C-terminus, including the loss of the NBD2 domain. AQ-C2 exhibited 20.2-fold greater resistance to Cry1Ac than the susceptible strain, and its inheritance of Cry1Ac resistance was recessive and genetically linked to PgABCC2. When produced in cultured insect cells, recombinant wild-type and r(C2) mutant PgABCC2 proteins localized within the cell plasma membrane, although substantial cytoplasmic retention was also observed for the mutant protein, while the mutant PgABCC2 caused a 13.9-fold decrease in Cry1Ac toxicity versus the wild-type PgABCC2. CONCLUSIONS: PgABCC2 is a functional receptor of Cry1Ac and the loss of its carboxyl terminus (including its NBD2 domain) confers low-level resistance to Cry1Ac in both larvae and in cultured cells. (c) 2024 Society of Chemical Industry.

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