Characterization and expression patterns of a membrane-bound trehalase from Spodoptera exigua

Tang, Bin; Chen, Xiaofei; Liu, Yang; Tian, He; Liu, Jian; Hu, Jian; Xu, Wei‐Hua; Zhang, Wenqing

doi:10.1186/1471-2199-9-51

Cited by 89 publications

(115 citation statements)

References 41 publications

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“…Trehalase catalyzes the conversion of the disaccharide trehalose into two glucose monomers. Two types of trehalases (soluble and membrane bound) are encoded in the S. exigua genome; the membrane-bound trehalase has been characterized in the midgut and fat body (Tang et al, 2008). The slight decrease of trehalose titer in the hemolymph of S. exigua in the current study may have been induced by the shutdown of trehalose biosynthesis in fat body as well as by the continuous usage by peripheral tissues.…”

Section: Discussionmentioning

confidence: 79%

RNA interference of glycerol biosynthesis suppresses rapid cold hardening of the beet armyworm,Spodoptera exigua

Park

Kim

2013

Journal of Experimental Biology

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SUMMARYThe beet armyworm, Spodoptera exigua, is a freeze-susceptible species that overwinters in temperate zones without diapause. A rapid cold hardening (RCH) and supercooling capacity usually play crucial roles in survival during the overwintering period. This study identified a cryoprotectant as a RCH factor of S. exigua. Pre-exposure of S. exigua larvae to 4°C significantly increased survival at −10°C in all developmental stages from egg to adult. RCH was dependent on the duration of the pre-exposure period. RCH also significantly enhanced the supercooling capacity. Cryoprotectant analysis using HPLC showed that the pre-exposure treatment allowed the larvae to accumulate glycerol in the hemolymph. Two genes, glycerol-3-phosphate dehydrogenase (GPDH) and glycerol kinase (GK), were identified as being associated with glycerol biosynthesis, and were cloned from S. exigua larvae. Both GPDH and GK were expressed in all developmental stages of S. exigua. RNA interference (RNAi) of either GPDH or GK significantly inhibited glycerol accumulation in the hemolymph of S. exigua. Larvae treated with RNAi for GPDH or GK exhibited a significant decrease in RCH capacity. The glycerol accumulation in response to 4°C appeared to be under the control of a humoral signal, because a ligation experiment prevented glycerol accumulation in the other half of the body. This study indicates that glycerol is a RCH factor of S. exigua and its synthesis is in response to low temperature via humoral mediation. Supplementary material available online at

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Section: Discussionmentioning

confidence: 79%

RNA interference of glycerol biosynthesis suppresses rapid cold hardening of the beet armyworm,Spodoptera exigua

Park

Kim

2013

Journal of Experimental Biology

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“…Trehalase (encoded by 2 genes, Treh1 and Treh2) is an anomer-inverting α-trehalose-1-D-glucosidase, which plays an important role in the use of carbohydrates by hydrolyzing trehalose molecules into 2 glucose molecules (Tang et al, 2008). To date, 2 forms of trehalase have been found and cloned in several insect species (Wyatt, 1967), including Apis mellifera (Lee et al, 2007), Bombyx mori (Mitsumasu et al, 2005), Omphisa fuscidentalis (Tatun et al, 2008), Pimpla hypochondriaca (Parkinson et al, 2003), Spodoptera exigua (Tang et al, 2008), and Tenebrio molitor (Takiguchi et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

“…To date, 2 forms of trehalase have been found and cloned in several insect species (Wyatt, 1967), including Apis mellifera (Lee et al, 2007), Bombyx mori (Mitsumasu et al, 2005), Omphisa fuscidentalis (Tatun et al, 2008), Pimpla hypochondriaca (Parkinson et al, 2003), Spodoptera exigua (Tang et al, 2008), and Tenebrio molitor (Takiguchi et al, 1992). Initial studies of trehalose and protein purification have found that the main distribution of soluble trehalase (Treh1) and membrane-bound trehalase (Treh2) sometimes differed (Tang et al, 2008), which might indicate different functions.…”

Section: Introductionmentioning

confidence: 99%

cDNA cloning and characterization of two trehalases from Spodoptera litura (Lepidoptera; Noctuidade)

Qi¹,

Wei²,

Xu³

et al. 2013

Genet. Mol. Res.

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ABSTRACT. The oriental leafworm moth, Spodoptera litura, is a major agricultural pest in southeast Asia and nearby Pacific regions. Two distinct trehalases have been identified in insects: soluble trehalase (Treh1) and membrane-bound trehalase (Treh2), although there is currently no information on these genes in S. litura. To characterize the distribution and function of treh, cDNAs of Treh proteins were cloned from S. litura. SpoliTreh1 cDNA has an open reading frame of 1758 nucleotides, which encodes a protein of 585 amino acids, with a predicted mass of approximately 67.07 kDa and an isoelectric point of 4.86. SpoliTreh2 cDNA has an open reading frame of 2325 nucleotides, encoding a protein of 645 amino acids, a mass of approximately 73.62 kDa, and an isoelectric point of 5.90. Northern blotting analysis revealed that SpoliTreh1 transcripts are in the midgut, fat body, tracheae, and epidermis, but not in the brain and Malpighian tubules of S. litura larvae, whereas SpoliTreh2 transcripts were found in all 6 tissues. SpoliTreh1 transcripts were highly expressed in the fat body of the prepupal stage, and SpoliTreh2 transcripts were highly expressed in the fat body of 3-day-old larvae of the 6th instar and during the 1st 6 days of the pupal stage, except the 2nd day. Both SpoliTreh1 and SpoliTreh2 were highly expressed in third-instar larvae.

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“…Membranes were prehybridized at 42°C for 4 h and then incubated with the -32 Plabelled CpiTPS probe (same probe as described for Southern blotting) at 42°C for 18 h in 5× SSPE containing 50% formamide, 5× Denhardt's solution, 0.1% SDS, and 100 mg/ml salmon sperm DNA. After hybridization, the membrane was washed with 0.2× SSPE at 45°C, and exposed to X-ray film at -70°C for 24 h (Choo et al, 2007;Tang et al, 2008).…”

Section: Northern Blot and Rt-pcr Analysismentioning

confidence: 99%

“…It is synthesized mainly by the fat body (an organ analogous in function to a combination of the liver and adipose tissue in vertebrates) and is released rapidly into the hemolymph and other tissues in larvae, pupae, and adults (Candy & Kilby, 1959, 1961Elbein, 1974;Becker et al, 1996;Tang et al, 2008). It is reported that trehalose is synthesized from glucose phosphate.…”

Section: Introductionmentioning

confidence: 99%

Cloning and pattern of expression of trehalose-6-phosphate synthase cDNA from Catantops pinguis (Orthoptera: Catantopidae)

Tang¹,

Zheng²,

Xu³

et al. 2011

Eur. J. Entomol.

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Abstract.Trehalose is not only an important disaccharide, but also a key stress resistance factor in the development of many organisms, including plants, bacteria, fungi, and insects. To study the potential function of trehalose in development and behaviour, cDNA for a trehalose-6-phosphate synthase from Catantops pinguis (CpiTPS) was cloned and sequenced. Results revealed that the CpiTPS cDNA sequence contains an open reading frame of 2430 nucleotides encoding a protein of 809 amino acids with a predicted molecular weight of 91.13 kDa and a pI value of 6.25. Northern blot and RT-PCR analyses showed that CpiTPS mRNA expression was high in the fat body and testes, ovaries, Malpighian tubules, brain, trachea, rectum, and posterior extensor of C. pinguis. Northern blotting revealed that CpiTPS mRNA was expressed in the fat body at different developmental stages and was present at a high level in first instar larvae and adults. The results demonstrate that CpiTPS is a key gene in C. pinguis development.

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Characterization and expression patterns of a membrane-bound trehalase from Spodoptera exigua

Cited by 89 publications

References 41 publications

RNA interference of glycerol biosynthesis suppresses rapid cold hardening of the beet armyworm,Spodoptera exigua

RNA interference of glycerol biosynthesis suppresses rapid cold hardening of the beet armyworm,Spodoptera exigua

cDNA cloning and characterization of two trehalases from Spodoptera litura (Lepidoptera; Noctuidade)

Cloning and pattern of expression of trehalose-6-phosphate synthase cDNA from Catantops pinguis (Orthoptera: Catantopidae)

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