ArticleBMC molecular biology2008
Characterization and expression patterns of a membrane-bound trehalase from Spodoptera exigua.
Article in BMC molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 98 citations in OpenAlex.
- A bacterial symbiont and a plant virus enhance insect fitness by inducing physical defenses against fungal parasites.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification, expression profiling, and functional characterization of trehalase genes (OaTRE1 and OaTRE) in Oedaleus asiaticus (Orthoptera: Acridoidea).Journal of insect science (Online) · 2026Article
- A taste of one's own medicine:Frontiers in immunology · 2025Article
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- Glucose influence cold tolerance in the fall armyworm, Spodoptera frugiperda via trehalase gene expression.Scientific reports · 2024Article
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- Steroid hormone-dependent changes in trehalose physiology in the silkworm, Bombyx mori.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Article
- Knockdown of Two Trehalase Genes by RNA Interference Is Lethal to the White-Backed PlanthopperBiomolecules · 2022Article
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- C/EBPα RegulatesInsects · 2022Article
- The Role of Insulin-like Peptide in Maintaining Hemolymph Glucose Homeostasis in the Pacific White ShrimpInternational journal of molecular sciences · 2022Article
- Purification and Characterization of Trehalase From Acyrthosiphon pisum, a Target for Pest Control.The protein journal · 2022Article
- Characterization and Functional Analysis ofInsects · 2021Article
- RNA Interference-Based Silencing of theInsects · 2020Article
- Gene Characterization and Enzymatic Activities Related to Trehalose Metabolism of In Vitro RearedInsects · 2020Article
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- The Modulation of Trehalose Metabolism by 20-Hydroxyecdysone in Antheraea pernyi (Lepidoptera: Saturniidae) During its Diapause Termination and Post-Termination Period.Journal of insect science (Online) · 2020Article
- Identification and Functional Analysis of Two Chitin Synthase Genes in the Common Cutworm,Insects · 2020Article
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- Three novel trehalase genes from3 Biotech · 2019Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe chitin biosynthesis pathway starts with trehalose in insects and the main functions of trehalases are hydrolysis of trehalose to glucose. Although insects possess two types, soluble trehalase (Tre-1) and membrane-bound trehalase (Tre-2), very little is known about Tre-2 and the difference in function between Tre-1 and Tre-2.
resultsTo gain an insight into trehalase functions in insects, we investigated a putative membrane-bound trehalase from Spodoptera exigua (SeTre-2) cloned from the fat body. The deduced amino acid sequence of SeTre-2 contains 645 residues and has a predicted molecular weight of approximately 74 kDa and pI of 6.01. Alignment of SeTre-2 with other insect trehalases showed that it contains two trehalase signature motifs and a putative transmembrane domain, which is an important characteristic of Tre-2. Comparison of the genomic DNA and cDNA sequences demonstrated that SeTre-2 comprises 13 exons and 12 introns. Southern blot analysis revealed that S. exigua has two trehalase genes and that SeTre-2 is a single-copy gene. Northern blot analyses showed that the SeTre-2 transcript is expressed not only in the midgut, as previously reported for Bombyx mori, but also in the fat body and Malpighian tubules, although expression patterns differed between the midgut and fat body. SeTre-2 transcripts were detected in the midgut of feeding stage larvae, but not in pupae, whereas SeTre-2 mRNA was detected in the fat body of fifth instar larvae and pupae.
conclusionThese findings provide new data on the tissue distribution, expression patterns and potential function of membrane-bound trehalase. The results suggest that the SeTre-2 gene may have different functions in the midgut and fat body.
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