Spirometra erinaceieuropaei
Ontology highlight
ABSTRACT:
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| DRR197402_1.fastq.gz | Fastqsanger.gz | |||
| DRR197402_2.fastq.gz | Fastqsanger.gz | |||
| DRR197403_1.fastq.gz | Fastqsanger.gz | |||
| DRR197403_2.fastq.gz | Fastqsanger.gz | |||
| DRR197404_1.fastq.gz | Fastqsanger.gz |
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Project description:Spirometra erinaceieuropaei overview
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Project description:Spirometra erinaceieuropaei Transcriptome or Gene expression
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Project description:Spirometra erinaceieuropaei Transcriptome or Gene expression
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Project description:Genome and transcriptome sequencing of Spirometra erinaceieuropaei
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Project description:Background: Sparganosis caused by Spirometra erinaceieuropaei spargana is a zoonotic parasitic infection which has been reported in many countries, such as China, Japan, Thailand and Korea, as well as the Europe and United States. This parasite biological and clinical significances, genome, and transcriptome analysis have previously been investigated, but its phosphoproteomes have not been reported. Here, we investigated global and site-specific phosphoproteome profiling of the spargana. Results: 3228 phosphopeptides and 3461 phosphorylation sites were identified from 1758 spargana proteins. The annotated phosphoproteins were involved in the various biological mechanisms, which included the cellular, metabolic and single-organism processes. Additionally, functional enrichment of phosphopepetides in Gene Ontology analysis suggested that most spargana phosphoproteins were related to the cytoskeleton cellular compartment, the signaling molecular function, and a variety of biological processes, including a molecular function regulator, guanyl-nucleotide exchange factor activity, protein kinase activities, and calcium ion binding. The highly enriched pathway of phosphorylation proteins included the phosphatidylinositol signaling system, phagosome, endocytosis, inositol phosphate metabolism, terpenoid backbone biosynthesis, and peroxisome pathways. Domain analysis of phosphopeptides identified EF-hand domain and pleckstrin homology domain among the important domains. Conclusions: This study provides the first global phosphoproteomic analysis in the spargana. The reported dataset will shed light on future understanding of zoonotic parasite.
2020-05-26 | PXD015753 | Pride
Project description:Genomic assembly of cestode Spirometra erinaceieuropaei, as part of the 50 Helminth Genomes Initiative sequencing of the parasitic worms that have the greatest impact on human, agricultural and veterinary disease and cause significant global health issues particularly in the developing world, or those used as model organisms.
| PRJEB1202 | ENA
Project description:Spirometra sp. Aus1 isolate:Aus1 Genome sequencing
| PRJNA938977 | ENA
Project description:Human sparganosis is a food-borne parasitic disease caused by the plerocercoids of Spirometra species. Clinical diagnosis of sparganosis is crucial for effective treatment, thus it is important to identify sensitive and specific antigens of plerocercoids. The aim of the current study was to identify and characterize the immunogenic proteins of Spirometra erinaceieuropaei plerocercoids that were recognized by patient sera. Crude soluble extract of the plerocercoids were separated using 2-dimensional gel electrophoresis coupled with immunoblot and mass spectrometry analysis. Based on immunoblotting patterns and mass spectrometry results, 8 antigenic proteins were identified from the plerocercoid. Among the proteins, cysteine protease protein might be developed as an antigen for diagnosis of sparganosis.
| S-EPMC8721309 | biostudies-literature
Project description:The present study was performed to compare the mitochondrial genomes between 2 Spirometra tapeworms, Spirometra erinaceieuropaei and Spirometra decipiens (Cestoidea: Diphyllobothriidae), which larval stages are important etiological agents of sparganosis in humans. For each species, the full mitochondrial genome was amplified in 8 overlapping fragments using total genomic DNA purified from a single worm as the template. The mitochondrial genomes were 13,643 bp (S. erinaceieuropaei) and 13,641 bp (S. decipiens) in length and contained 36 genes; 12 protein-coding genes, 2 ribosomal RNA (rRNA, small and large subunits), and 22 transfer RNAs (tRNAs). The 12 protein-coding genes constituted 10,083 bp (S. erinaceieuropaei) and 10,086 bp (S. decipiens) of their respective mitochondrial genomes. The tRNA genes, ranging in length from 56 to 70 bp, were identified based on putative secondary structures such as the typical cloverleaf shape. A total of 23 intergenic sequences, varying from 1 to 204 bp in size, were interspersed in S. erinaceieuropaei (total, 504 bp) and S. decipiens (total, 496 bp) mtDNA. The 12 protein-coding genes of S. erinaceieuropaei and S. decipiens differed by 12.4%, whereas the overall difference in mtDNA sequence between S. erinaceieuropaei and S. decipiens was 12.9%. Thus, from the standpoint of the mitochondrial genome, S. decipiens represents a valid species that can be distinguished from S. erinaceieuropaei.
| S-EPMC4566511 | biostudies-literature
Project description:BackgroundSparganosis caused by Spirometra erinaceieuropaei spargana is a zoonotic parasitic infection that has been reported in many countries, including China, Japan, Thailand and Korea, as well as European countries and the USA. The biological and clinical significance of the parasite have previously been reported. Although the genomic and transcriptomic analysis of S. erinaceieuropaei provided insightful views about the development and pathogenesis of this species, little knowledge has been acquired in terms of post-translational regulation that is essential for parasite growth, development and reproduction. Here, we performed site-specific phosphoproteomic profiling, with an aim to obtain primary information about the global phosphorylation status of spargana.ResultsA total of 3228 phosphopeptides and 3461 phosphorylation sites were identified in 1758 spargana proteins. The annotated phosphoproteins were involved in a variety of biological pathways, including cellular (28%), metabolic (20%) and single-organism (17%) processes. The functional enrichment of phosphopeptides by Gene Ontology analysis indicated that most spargana phosphoproteins were related to the cytoskeleton cellular compartment, signaling molecular function, and a variety of biological processes, including a molecular function regulator, guanyl-nucleotide exchange factor activity, protein kinase activities, and calcium ion binding. The highly enriched pathways of phosphorylation proteins include the phosphatidylinositol signaling system, phagosome, endocytosis, inositol phosphate metabolism, terpenoid backbone biosynthesis, and peroxisome. Domain analysis identified an EF-hand domain and pleckstrin homology domain among the key domains.ConclusionsTo our knowledge, this study performed the first global phosphoproteomic analysis of S. erinaceieuropaei. The dataset reported herein provides a valuable resource for future studies on the signaling pathways of this important zoonotic parasite.
| S-EPMC7218563 | biostudies-literature