Abstract
ATP-binding cassette (ABC) transporters, a large class of transmembrane proteins, are widely found in organisms and play an important role in the transport of xenobiotics. Insect ABC transporters are involved in insecticide detoxification and Bacillus thuringiensis (Bt) toxin perforation. The complete ABC transporter is composed of two hydrophobic transmembrane domains (TMDs) and two nucleotide binding domains (NBDs). Conformational changes that are needed for their action are mediated by ATP hydrolysis. According to the similarity among their sequences and organization of conserved ATP-binding cassette domains, insect ABC transporters have been divided into eight subfamilies (ABCA–ABCH). This review describes the functions and mechanisms of ABC transporters in insecticide detoxification, plant toxic secondary metabolites transport and insecticidal activity of Bt toxin. With improved understanding of the role and mechanisms of ABC transporter in resistance to insecticides and Bt toxins, we can identify valuable target sites for developing new strategies to control pests and manage resistance and achieve green pest control.
Highlights
ATP-binding cassette (ABC) proteins comprise an extensive and variable transporter superfamily within P-loop motif and are found in all living organisms [1,2,3]
Excellent reviews on the role of insect ABC transporters in the transport and resistance to Bacillus thuringiensis (Bt) toxin and insecticide have been published previously [14,27,28], so the present review provides an update of our understanding of the evolution, function and role of the ABC transporter superfamily of insects in xenobiotic transport and detoxification
According to the distinctive conserved traits, ABCA subfamily proteins can be divided into full transporters (FTs) and half transporters (HTs); the number of insect ABCA genes differs among different species (3–15)
Summary
ATP-binding cassette (ABC) proteins comprise an extensive and variable transporter superfamily within P-loop motif and are found in all living organisms [1,2,3]. The primary function of most ABC proteins is ATP-dependent active transport of a broad spectrum of substrates including amino acids, sugars, heavy metal ions and conjugates, peptides, lipids, polysaccharides, xenobiotics and chemotherapeutic drugs across cellular membranes [1,12,13,14], but they are involved in many other biochemical and physiological processes. In humans, they have been shown to function as ion channels and receptors [1,12,15]. Excellent reviews on the role of insect ABC transporters in the transport and resistance to Bt toxin and insecticide have been published previously [14,27,28], so the present review provides an update of our understanding of the evolution, function and role of the ABC transporter superfamily of insects in xenobiotic transport and detoxification
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