Dataset Information

Cloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus.

ABSTRACT: Insect trehalase is a multiferous enzyme, crucial for normal physiological functions as well as under stress conditions. In this report, we present a fundamental study of the trehalase gene segment (1587 bp) from Chironomus ramosus (CrTre) encoding for 529 amino acids, using appropriate bioinformatics tools. C. ramosus, a tropical midge is an emerging animal model to investigate the consequences of environmental stresses. We observed that CrTre belongs to GH family 37 in the CAZy database and possess 57-92% identity to dipteran trehalases. In silico characterization provided information regarding the structural, functional and evolutionary aspects of midge trehalase. In the phylogenetic tree, CrTre clustered with the soluble dipteran trehalases. Moreover, domain functional characterization of the deduced protein sequence by InterProScan (IPR001661), ProSite (PS00927 and PS00928) and Pfam (PF01204) indicated presence of highly conserved signature motifs which are important for the identification of trehalase superfamily. Furthermore, the instability index of CrTre was predicted to be

SUBMITTER: Shukla E

PROVIDER: S-EPMC6070458 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Cloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus.

Shukla Ekta E Thorat Leena L Bendre Ameya D AD Jadhav Santosh S Pal Jayanta K JK Nath Bimalendu B BB Gaikwad Sushama M SM

3 Biotech 20180801 8

Insect trehalase is a multiferous enzyme, crucial for normal physiological functions as well as under stress conditions. In this report, we present a fundamental study of the trehalase gene segment (1587 bp) from Chironomus ramosus (CrTre) encoding for 529 amino acids, using appropriate bioinformatics tools. C. ramosus, a tropical midge is an emerging animal model to investigate the consequences of environmental stresses. We observed that CrTre belongs to GH family 37 in the CAZy d ...[more]

PMID: 30105177

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Project description:This study focuses on interactions between nanoparticles and a pesticide. The aim was to investigate how nano-sized aluminum oxide (410 nm) can alter the toxic effects of thiacloprid, even if no sorption between particles and the insecticide takes place. Thus, our study investigated a rather unexplored interaction. We conducted our research with larvae of Chironomus riparius and used thiacloprid as test substance as its toxicity to C. riparius is well described. The used nano-Al2O3 particles where chosen due to their suitable properties. For testing the acute effects of the interaction, we exposed larvae to thiacloprid (0.5, 1.0, 2.0, and 5.0 μg/L) and nano-Al2O3 (300 and 1000 mg/L), either solely or in binary mixtures. While thiacloprid resulted in elevated mortality, nano-Al2O3 solely did not exert any effects. Moreover, we observed an aggregation of nano-Al2O3 within the lumen of the intestinal tract of the larvae. Further results showed a significantly reduced mortality of fourth instar larvae when they were exposed to mixtures of nanoparticles and the pesticide, compared to thiacloprid alone. With increasing nano-Al2O3 concentration, this effect became gradually stronger. Additionally, chemical analyses of internal thiacloprid concentrations implicate reduced uptake of thiacloprid in animals exposed to mixtures. However, as larvae exposed to thiacloprid concentrations > 0.5 μg/L showed severe convulsions, independent of the presence or concentration of nano-Al2O3, we assume that nano-Al2O3 leads to a delay of mortality and does not entirely prevent it. As sorption measurements on pristine or defecated nano-Al2O3 did not reveal any sorptive interaction with thiacloprid, we can exclude sorption-based reduction of thiacloprid bioavailability as a mechanism behind our results. Even though we used test substances which might not co-occur in the environment in the tested concentrations, our study gives evidence for an interaction besides adsorption, which is important to generally understand how nanoparticles might affect biota.

Project description:Background Representatives of the family Chironomidae (non-biting midges; order Diptera) are found worldwide. Freeze-dried chironomid larvae, predominantly of the species Chironomus thummi thummi are frequently used as fish food and are an allergen source for fish keepers and persons employed in the manufacture of fish food. At present, 9 allergens of C. thummi thummi have been assigned an official designation by the WHO/IUIS allergen nomenclature sub-committee: Chi t 1 to 9. All of them are hemoglobins with molecular weights of 16 kDa. IgE binding and cross-reactivity was clearly demonstrated for all these proteins. However, the assignment of 9 distinct allergen numbers to members of the same protein family is quite unusual. Methods Currently, the IUIS allergen database contains 12 allergen and isoallergen sequences from C. thummi thummi. The Uniprot database has demerged entry P02225, listed in the database for Chi t 7, into 7 entries, 5 from C. thummi thummi and 2 from C. thummi piger that are identical to 2 of the sequences from C. thummi thummi. Consequently, the 16 unique amino acid sequences of the mature C. thummi allergens were aligned using ClustalX2, a neighbor-joining tree was generated from the alignment and a percent sequence identity matrix was built to evaluate appropriate nomenclature. Results Pairwise sequence alignments showed that sequences belonging to allergens Chi t 5, 6, 7 and 8 possess sequence identities to Chi t 3 of between 51 and 63%. Chi t 1, 2, 4, and 9 diverge to a greater extent from Chi t 3 (<50% identical) and from each other. Phylogenetic tree analysis suggests the clustering of Chi t 3, 6, 7, and 8, while Chi t 1, 2, 4, 5, and 9 form separate clades. Conclusions Based on these analyses, the IUIS Allergen Nomenclature Sub-Committee renames Chi t 5, 6, 7 and 8 isoallergens of Chi t 3, even though their sequence identities to Chi t 3 are below the 67% threshold previously defined for isoallergens. The remaining hemoglobins, previously designated Chi t 1, 2, 4 and 9 will retain their previous names.

Dataset Information

Cloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus.

Publications

Cloning and characterization of trehalase: a conserved glycosidase from oriental midge, <i>Chironomus ramosus</i>.

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