UDP-glycosyltransferase genes and their association and mutations associated with pyrethroid resistance in Anopheles sinensis (Diptera: Culicidae)

Abstract

Background UDP-glycosyltransferase (UGT) is an important biotransformation superfamily of enzymes. They catalyze the transfer of glycosyl residues from activated nucleotide sugars to acceptor hydrophobic molecules, and function in several physiological processes, including detoxification, olfaction, cuticle formation, pigmentation. The diversity, classification, scaffold location, characteristics, phylogenetics, and evolution of the superfamily of genes at whole genome level, and their association and mutations associated with pyrethroid resistance are still little known. Methods The present study identified UGT genes in Anopheles sinensis genome, classified UGT genes in An. sinensis , Anopheles gambiae , Aedes aegypti and Drosophila melanogaster genomes, and analysed the scaffold location, characteristics, phylogenetics, and evolution of An. sinensis UGT genes using bioinformatics methods. The present study also identified the UGTs associated with pyrethroid resistance using three field pyrethroid-resistant populations with RNA-seq and RT-qPCR, and the mutations associated with pyrethroid resistance with genome re-sequencing in An. sinensis . Results There are 30 putative UGTs in An. sinensis genome, which are classified into 12 families (UGT301, UGT302, UGT306, UGT308, UGT309, UGT310, UGT313, UGT314, UGT315, UGT36, UGT49, UGT50) and further into 23 sub-families. The UGT308 is significantly expanded in gene number compared with other families. A total of 119 UGTs from An. sinensis , An. gambiae , Aedes aegypti and Drosophila melanogaster genomes are classified into 19 families, of which seven are specific for three mosquito species and seven are specific for Drosophila melanogaster . The UGT308 and UGT302 are proposed to main families involved in pyrethroid resistance. The AsUGT308D3 is proposed to be the essential UGT gene for the participation in biotransformation in pyrethroid detoxification process, which is possibly regulated by eight SNPs in its 3′ flanking region. The UGT302A3 is also associated with pyrethroid resistance, and four amino acid mutations in its coding sequences might enhance its catalytic activity and further result in higher insecticide resistance. Conclusions This study provides the diversity, phylogenetics and evolution of UGT genes, and potential UGT members and mutations involved in pyrethroid resistance in An. sinensis , and lays an important basis for the better understanding and further research on UGT function in defense against insecticide stress. ...

Genome-Wide Identification and Expression Analysis of Udp-Glucuronosyltransferases in the Whitefly Bemisia Tabaci (Gennadius) (HemipterA: Aleyrodidae)

“…Insect UGT genes play diverse roles, including detoxification, digestion, olfaction and pigmentation and they are expressed in many different tissues [15,43]. The over-expressions of UGT genes in insecticide-resistant insects have been reported in Leptinotarsa decemlineata (Say), Plutella xylostella (L.), Diaphorina citri Kuwayama, Tetranychus cinnabarinus (Boisduval), Anopheles sinensis Wiedemann and Aphis gossypii Glover [43][44][45][46][47][48]. It has also been reported that UGTs were induced by insecticide exposures in Spodoptera exigua (Hübner) and Bemisia tabaci (Gennadius) [49,50].…”

Anopheles metabolic proteins in malaria transmission, prevention and control: a review

“…In a recent study on An. sinensis, upregulated expression of UGT308D3 and UGT302A3 were associated with pyrethroid resistance [118]. In Cx.…”

Modulation of Sex Pheromone Discrimination by a UDP-Glycosyltransferase in Drosophila melanogaster

“…Although phase II enzymes are expected to play a similar role as phase I enzymes in the metabolism of plant volatiles, pheromones or diverse odorants [9,16,20,22], no olfactory function was revealed so far in insects. Among phase II ODEs, the study of UGTs received an increasing interest during the last decade, especially with regard to insecticide resistance and plant defense mechanisms [37][38][39][40][41][42][43][44]. This major class of enzymes in the animal kingdom [45,46] catalyzes in insects the conjugation of a glycosyl group brought by a UDP-glycoside to hydrophobic substrates [47,48].…”