The catalytic and other residues essential for the activity of the midgut trehalase from Spodoptera frugiperda

Silva, Maria C. P.; Terra, Walter R.; Ferreira, Clélia

doi:10.1016/j.ibmb.2010.07.006

Cited by 34 publications

(35 citation statements)

References 40 publications

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“…Trehalose is present in almost all forms of life except mammals (Lee et al, 2001;Elbein et al, 2003;Frison et al, 2007;Silva et al, 2010). It protects cellular membranes and proteins from oxidation, dehydration, heat, freezing, desiccation, and cold owing to its higher glass transition temperature compared with those to other sugars (Crowe et al, 1984;Eleutherio et al, 1993;Sun and Davidson, 1998;Davidson and Sun, 2001).…”

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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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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“…Unlike glucose in mammals, the major blood (hemolymph) sugar of insects is often the disaccharide trehalose (α-D-glucopyranosyl-α-D-glucopyranoside) [4]–[6]. It is synthesized from glucose phosphates in fat body tissue and serves as a source of carbohydrates for various tissues including flight muscles [7], [8], intestinal tract [9], fat body [10] or ovaries [11]. Besides trehalose absorption, the absorption of other sugars, such as fructose, glucose, and galactose, has been shown for different insect tissues [12]–[17].…”

Section: Introductionmentioning

confidence: 99%

Putative Sugar Transporters of the Mustard Leaf Beetle Phaedon cochleariae: Their Phylogeny and Role for Nutrient Supply in Larval Defensive Glands

et al. 2013

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BackgroundPhytophagous insects have emerged successfully on the planet also because of the development of diverse and often astonishing defensive strategies against their enemies. The larvae of the mustard leaf beetle Phaedon cochleariae, for example, secrete deterrents from specialized defensive glands on their back. The secretion process involves ATP-binding cassette transporters. Therefore, sugar as one of the major energy sources to fuel the ATP synthesis for the cellular metabolism and transport processes, has to be present in the defensive glands. However, the role of sugar transporters for the production of defensive secretions was not addressed until now.ResultsTo identify sugar transporters in P. cochleariae, a transcript catalogue was created by Illumina sequencing of cDNA libraries. A total of 68,667 transcripts were identified and 68 proteins were annotated as either members of the solute carrier 2 (SLC2) family or trehalose transporters. Phylogenetic analyses revealed an extension of the mammalian GLUT6/8 class in insects as well as one group of transporters exhibiting distinctive conserved motifs only present in the insect order Coleoptera. RNA-seq data of samples derived from the defensive glands revealed six transcripts encoding sugar transporters with more than 3,000 counts. Two of them are exclusively expressed in the glandular tissue. Reduction in secretions production was accomplished by silencing two of four selected transporters. RNA-seq experiments of transporter-silenced larvae showed the down-regulation of the silenced transporter but concurrently the up-regulation of other SLC2 transporters suggesting an adaptive system to maintain sugar homeostasis in the defensive glands.ConclusionWe provide the first comprehensive phylogenetic study of the SLC2 family in a phytophagous beetle species. RNAi and RNA-seq experiments underline the importance of SLC2 transporters in defensive glands to achieve a chemical defense for successful competitive interaction in natural ecosystems.

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“…Branches corresponding to partitions reproduced in under 50% of bootstrap replicates were collapsed. Homology modelling was performed using the server Phyre (Kelley & Sternberg, 2009) and SWISS-MODEL (Arnold et al, 2006) and the results were analysed with PYMOL (De Lano Scientific, LLC, Bielefeld, Germany) and MOLPROBITY (Chen et al, 2010), as described in Silva et al (2010). fellow of FAPESP and I. Bragatto a graduate fellow of CNPq. C. Ferreira and W. R. Terra are staff members of their departments, research fellows of the CNPq and members of the Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular.…”

Section: Computational Analysis Of Sequencesmentioning

confidence: 99%

Insect midgut carboxypeptidases with emphasis on S10 hemipteran and M14 lepidopteran carboxypeptidases

Ferreira

Rebola

Cardoso

et al. 2014

Insect Molecular Biology

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We compared the whole complement of midgut carboxypeptidases from 10 insects pertaining to five orders based on transcriptomes obtained by deep sequencing and biochemical data. Most of the carboxypeptidases were metallocarboxypeptidases from family M14, with carboxypeptidase A (CPA) predominating over carboxypeptidase B (CPB). They were found in all of the insects studied except for the hemipterans and a bruchid beetle. M14 carboxypeptidases were expressed only in the midgut of Spodoptera frugiperda (Lepidoptera). The most expressed CPA from this insect (SfCPA) was cloned, sequenced and expressed as a recombinant enzyme. This enzyme was used to generate antibodies used to demonstrate that SfCPA is secreted by an exocytic route. Serine carboxypeptidases from family S10 were found in all of the insects studied here. In S. frugiperda, they are expressed in all tissues besides the midgut, in accordance with their presumed lysosomal role. In the hemipteran Dysdercus peruvianus, S10 carboxypeptidases are expressed only in midgut, suggesting that they are digestive enzymes. This was confirmed by enzyme assays of midgut contents. Furthermore, the substrate specificity of D. peruvianus S10 carboxypeptidases are predicted to be one CPC (preferring hydrophobic residues) and one CPD (preferring basic residues), thus able to hydrolyse the peptides formed by their digestive cathepsin D and cathepsin L, respectively. The role of S10 carboxypeptidases in bruchid beetles are suggested to be the same as in hemipterans.

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The catalytic and other residues essential for the activity of the midgut trehalase from Spodoptera frugiperda

Cited by 34 publications

References 40 publications

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

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

Putative Sugar Transporters of the Mustard Leaf Beetle Phaedon cochleariae: Their Phylogeny and Role for Nutrient Supply in Larval Defensive Glands

Insect midgut carboxypeptidases with emphasis on S10 hemipteran and M14 lepidopteran carboxypeptidases

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