Abstract

Simple SummaryThe melon fly, Zeugodacus cucurbitae, is an important agricultural pest. At present, chemical pesticide treatment is the main method for field control, but this promotes pesticide resistance by Z. cucurbitae, because of its frequent use. ABC transporters are involved in detoxification metabolism, but few studies have yet considered their expression in melon fly. In this study, we identified the ABC transporters genes at a genome-wide level in melon fly, and analysed their spatiotemporal expression patterns, as well as changes in expression after insecticides treatments. A total of 49 ABC transporters were identified, and their expression levels varied at different developmental stages and between tissues. After three insecticides treatment, ZcABCB7 and ZcABCC2 were up-regulated. After β-cypermethrin induction, tissues were dissected at 12, 24 and 48 h, and the expression levels of a number of ABC genes were highly expressed within the fat body. From these results, we conclude that ZcABCB7 and ZcABCC2 may be involved in detoxification metabolism, and that the fat body is the main tissue that plays this role.The ATP-binding cassette (ABC) transporter is a protein superfamily that transports specific substrate molecules across lipid membranes in all living species. In insects, ABC transporter is one of the major transmembrane protein families involved in the development of xenobiotic resistance. Here, we report 49 ABC transporter genes divided into eight subfamilies (ABCA-ABCH), including seven ABCAs, seven ABCBs, 10 ABCCs, two ABCDs, one ABCE, three ABCFs, 16 ABCGs, and three ABCHs according to phylogenetic analysis in Zeugodacus cucurbitae, a highly destructive insect pest of cucurbitaceous and other related crops. The expressions level of 49 ABC transporters throughout various developmental stages and within different tissues were evaluated by quantitative transcriptomic analysis, and their expressions in response to three different insecticides were evaluated by quantitative real-time polymerase chain reaction (qRT-PCR). These ABC transporter genes were widely expressed at developmental stages but most highly expressed in tissues of the midgut, fat body and Malpighian tube. When challenged by exposure to three insecticides, abamectin, β-cypermethrin, and dinotefuran, the expressions of ZcABCB7 and ZcABCC2 were significantly up-regulated. ZcABCB1, ZcABCB6, ZcABCB7, ZcABCC2, ZcABCC3, ZcABCC4, ZcABCC5, and ZcABCC7 were significantly up-regulated in the fat body at 24 h after β-cypermethrin exposure. These data suggest that ZcABCB7 and ZcABCC2 might play key roles in xenobiotic metabolism in Z. cucurbitae. Collectively, these data provide a foundation for further analysis of ABCs in Z. cucurbitae.

Highlights

  • ATP-binding cassette (ABC) proteins comprise one of the largest superfamilies of prokaryote and eukaryote membrane proteins [1]

  • Based upon the genome sequence, we identified 49 putative ABC genes in Z. cucurbitae

  • These genes were divided into eight subfamilies: seven ABCAs, seven ABCBs, 10 ABCCs, two ABCDs, one ABCEs, three ABCFs, 16 ABCGs, and three ABCHs (Table 1), according to the highly conserved nucleotide-binding domain (NBD) of D. melanogaster ABC transporter genes

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Summary

Introduction

ATP-binding cassette (ABC) proteins comprise one of the largest superfamilies of prokaryote and eukaryote membrane proteins [1]. A total of 48 ABC transporters in humans are divided into seven subfamilies (ABCA to ABCG) [2], while in Drosophila melanogaster, an eighth subfamily (ABCH) was first discovered. This latter member is widely expressed in arthropods and zebrafish but not in mammals, plants and fungi [3,4]. The majority of these ABC proteins comprise two highly conserved structural domains, a nucleotide-binding domain (NBD) that can bind and hydrolyze ATP, and a transmembrane domain (TMD) that is comprised of six membrane-spanning helices [5]. These are either half-transporters which have one TMD and one NBD, or full-transporters which have two TMDs and two NBDs, and often form a functional unit as a homo- or heterodimer [1,6]

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