Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jprot.2013.06.017
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dc.titleThe transcriptome of Echinostoma caproni adults: Further characterization of the secretome and identification of new potential drug targets
dc.contributor.authorGarg, G.
dc.contributor.authorBernal, D.
dc.contributor.authorTrelis, M.
dc.contributor.authorForment, J.
dc.contributor.authorOrtiz, J.
dc.contributor.authorValero, M.L.
dc.contributor.authorPedrola, L.
dc.contributor.authorMartinez-Blanch, J.
dc.contributor.authorEsteban, J.G.
dc.contributor.authorRanganathan, S.
dc.contributor.authorToledo, R.
dc.contributor.authorMarcilla, A.
dc.date.accessioned2014-11-25T09:47:48Z
dc.date.available2014-11-25T09:47:48Z
dc.date.issued2013-08-26
dc.identifier.citationGarg, G., Bernal, D., Trelis, M., Forment, J., Ortiz, J., Valero, M.L., Pedrola, L., Martinez-Blanch, J., Esteban, J.G., Ranganathan, S., Toledo, R., Marcilla, A. (2013-08-26). The transcriptome of Echinostoma caproni adults: Further characterization of the secretome and identification of new potential drug targets. Journal of Proteomics 89 : 202-214. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jprot.2013.06.017
dc.identifier.issn18743919
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/108579
dc.description.abstractEchinostomes are cosmopolitan parasites that infect a large number of different warm-blooded hosts, both in nature and in the laboratory. They also constitute an important group of food-borne trematodes of public health importance mainly in Southeast Asia and the Far East.In addition, echinostomes are an ideal model to study several aspects of intestinal helminth biology, since they present a number of advantages. For example, echinostomes are large worms whose life cycle is relatively easy to maintain in the laboratory. Recently, several studies documented their great value in the study of intestinal helminth-vertebrate host relationship. Detailed knowledge of their genome, transcriptome and proteome is likely to have an important impact on the development of control strategies for intestinal helminths.We present the first transcriptome of the adult stage of Echinostoma caproni using 454 sequencing coupled to a semi-automated bioinformatic analyses. 557,236 raw sequence reads were assembled into 28,577 contiguous sequences using iAssembler. 23,296 putative proteins were characterized based on homology, gene ontology and/or biochemical pathways. Comparisons of the transcriptome of E. caproni with those of other trematodes revealed similarities in the transcription pattern of molecules inferred to have key roles in parasite-host interactions. Enzymatic proteins like kinases and peptidases were abundant. Of the 3415 predicted excretory/secretory proteins compiled (including non-classical secretory proteins), 180 different proteins were confirmed by proteomic analysis. Potential drug targets were also identified. Biological significance: In this study the first transcriptome of the adult stage of E. caproni is presented and compared to those of other trematodes revealing similarities in transcription for molecules inferred to have key roles in parasite-host interactions. 3415 predicted excretory/secretory proteins were compiled, being 180 different proteins confirmed by proteomic analysis. The current transcriptome data increased by nine times the number of previous protein identifications. In addition, potential drug targets for this parasite were identified. The present dataset should provide a solid foundation for future fundamental genomic, proteomic, and metabolomic explorations of E. caproni, as well as a basis for applied outcomes, such as the development of novel methods of intervention against this model organism and related parasites. © 2013 Elsevier B.V.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jprot.2013.06.017
dc.sourceScopus
dc.subjectDrug target
dc.subjectEchinostoma
dc.subjectProteomics
dc.subjectSecretome
dc.subjectTranscriptome
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/j.jprot.2013.06.017
dc.description.sourcetitleJournal of Proteomics
dc.description.volume89
dc.description.page202-214
dc.identifier.isiut000323867200017
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