Characterization and Expression Profiles of Juvenile Hormone Epoxide Hydrolase From Lymantria dispar (Lepidoptera: Lymantridae) and RNA Interference by Ingestion

Abstract

Juvenile hormone epoxide hydrolase (JHEH) is an important enzyme in the degradation pathways of juvenile hormone (JH) in insects. It converts JH to JH diol and hydrolyses JH acid to JH acid diol. JHEH titers regulate the entire process of insect development. In this study, full length ldjheh cDNA (2101 bp) was cloned from the Asian gypsy moth Lymantria dispar (L.; Lepidoptera: Lymantridae), and provisionally designated ldjheh1. LdJHEH1 was characterized by predicted molecular weight of 52.64 kDa, theoretical isoelectric points of 6.87 and contains a transmembrane domain at the N-terminus. The transcriptional profiles of ldjheh1 were detected by qRT-PCR. The ldjheh1 was found to be expressed throughout all developmental stages with maximum expression levels occurring in fourth instar larvae. The ldjheh1 mRNA was detected in the heads, thoraces, and abdomens of gypsy moth larvae on day 2 of the third instar. The ldjheh1 was also detected in bodies of third instar larvae stage, with the highest peaks occurring at 24 h after ecdysis. The ldjheh1 gene was successfully knocked down by oral delivery dsRNA in the third instar larvae of L. dispar. The dsRNA targeting ldjheh1 was produced in vitro. Ingesting dsRNA for ldjheh1 only slightly delayed larval development.

Cloning and Characterization of Drosophila melanogaster Juvenile Hormone Epoxide Hydrolases (JHEH) and Their Promoters

“…The cDNAs code for proteins of 474, 463 and 468 amino acids, respectively ( Figure 1 a–c). The proteins contain XWG anchor motif (W40, W41 and G42 for JHEH 1; Y41, W42 and G43 for JHEH 2 and Y42, W43 and G44 for JHEH 3) ( Figure 1 a–c), which is involved in subcellular localization of JHEH in Bombyx mori , Lymantria dispar and Apolygus lucorum , and is highly conserved in higher organisms, but absent in fungi, bacteria and protozoa [ 38 , 47 , 48 ]. JHEH 1, 2 and 3 amino acid sequences contain a HGWP motif and W166, W163 and W163 as part of the motif in JHEH 1, 2 and 3, respectively ( Figure 1 a–c).…”

Cloning and characterization of Aedes aegypti juvenile hormone epoxide hydrolases (JHEHs)

“…Ae. aegypti JHEH 1, 2, and 3 contain a HGWP motif that was also found in JHEHs of other insects (Borovsky et al, 2022;Seino et al, 2010;Wen et al, 2018) and W159 as part of the motif in JHEH 1, 2, and 3 (Figure 1a (Borovsky et al, 2022). The jheh of Ae.…”

“…aegypti (Tusun et al, 2017;. The cDNAs code for proteins of 461, 462, and 458 amino acids, melanogaster (Borovsky et al, 2022;Reetz et al, 2009;Tusun et al, 2017;Wen et al, 2018). Ae.…”

“…aegypti (Tusun et al, 2017; Van Ekert, Powell, et al, 2014). The cDNAs code for proteins of 461, 462, and 458 amino acids, respectively (Figure 1a−c), The proteins contain anchor XWG motif (Y40, W41, and G42 for JHEH 1, 2 and 3) (Figure 1a−c), which is involved in subcellular binding of JHEH in B. mori, Lymantria dispar, Apolygus lucorum and D. melanogaster (Borovsky et al, 2022; Reetz et al, 2009; Tusun et al, 2017; Wen et al, 2018). Ae.…”

Sublethal concentration of emamectin benzoate inhibits the growth of gypsy moth by inducing digestive dysfunction and nutrient metabolism disorder

“…Before hatching, the egg masses were soaked in formaldehyde for 30 min to disinfect. The larvae were reared on artificial diet at 25 °C under 14:10 (L:D) photoperiod and 65% relative humidity, as described previously 27 . The fifth‐instar larvae (healthy and similar in size) were selected for subsequent experiments.…”