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Previous issue date: 2012-08-31 / The two parasites in the genus Angionstrongylus that cause disease in humans are Angiostrongylus costarisensis and Angiostrongylus cantonensis. They have different target organs: A. costarisensis is located in the mesentery and causes eosinophilic ileocolitis, whereas A. cantonensis is a neurotropic parasite responsible for eosinophilic meningoencephalitis. Based on several indications that the sexual maturation is associated with increased pathogenesis in angiostrongylid worms, proteomic analysis was performed on A. cantonensis protein samples, to describe differential protein expression between 21 and 42 days post infection. Triplicated bidimensional electrophoresis was submitted to analysis and 11 proteins were found to be exclusively expressed after sexual maturation. Acetate kinase was the only protein that could be identified after mass spectrometry (LC-MS/MS). Since acetate is an important end-product of the energy metabolism among many parasites but not among their mammalian hosts, acetate formation is an attractive target for the development of new anti-parasitic drugs. Furthermore, studying the adaptations in parasite metabolisms can result in an increased understanding of the host-parasite interaction. This data open opportunities for control interventions and new strategies for molecular diagnosis. / Os principais parasitos do g?nero Angionstrongylus que causam doen?a nos seres humanos s?o Angiostrongylus costarisensis e Angiostrongylus cantonensis. Eles t?m distintos ?rg?os alvos: A. costarisensis est? localizado no mesent?rio e causa ileocolite eosinof?lica, enquanto que A. cantonensis ? um parasita neurotr?pico respons?vel pela meningoencefalite eosinof?lica. Com base em v?rias evid?ncias de que a matura??o sexual est? associada ao aumento da patog?nese em vermes deste g?nero, uma an?lise prote?mica foi realizada em vermes de A. cantonensis para descrever a express?o diferencial de prote?nas entre 21 e 42 dias ap?s a infec??o. Eletroforese bidimensional em triplicata foi submetida ? an?lise e 11 prote?nas foram encontradas exclusivamente expressas ap?s a matura??o sexual. A acetato quinase foi a ?nica prote?na identificada por espectrometria de massa (LC-MS/MS). O acetato ? um importante produto final do metabolismo energ?tico de muitos parasitos, mas n?o de seus hospedeiros mam?feros. Sendo assim, ? um alvo atrativo para o desenvolvimento de novas drogas anti-parasit?rias. Al?m do mais, o estudo das adapta??es no metabolismo do parasito pode resultar em uma maior compreens?o da rela??o parasito-hospedeiro. Este trabalho abre oportunidades para interven??es de controle e novas estrat?gias de diagn?stico molecular.
| Identifer | oai:union.ndltd.org:IBICT/oai:tede2.pucrs.br:tede/5451 |
| Date | 31 August 2012 |
| Creators | Oliveira, Camila Krug de |
| Contributors | Graeff-teixeira, Carlos |
| Publisher | Pontif?cia Universidade Cat?lica do Rio Grande do Sul, Programa de P?s-Gradua??o em Biologia Celular e Molecular, PUCRS, BR, Faculdade de Bioci?ncias |
| Source Sets | IBICT Brazilian ETDs |
| Language | Portuguese |
| Detected Language | English |
| Type | info:eu-repo/semantics/publishedVersion, info:eu-repo/semantics/masterThesis |
| Format | application/pdf |
| Source | reponame:Biblioteca Digital de Teses e Dissertações da PUC_RS, instname:Pontifícia Universidade Católica do Rio Grande do Sul, instacron:PUC_RS |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | 8198246930096637360, 600, 600, 36528317262667714 |
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