4.6 Article

Proteomic profiling of hydatid fluid from pulmonary cystic echinococcosis

期刊

PARASITES & VECTORS
卷 15, 期 1, 页码 -

出版社

BMC
DOI: 10.1186/s13071-022-05232-8

关键词

Echinococcus granulosus; Echinococcus ortleppi; Secretome; Hydatid fluid; Parasite proteomics; Host-parasite interface

资金

  1. Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [472316/2013-3, 470716/2014-2]
  2. Fundacao de Amparo a Pesquisa do Rio Grande do Sul (FAPERGS) [001892-25.51/13-0]
  3. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2013/07467-1]
  4. Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) [PARASITOLOGIA-1278/2011, Computacional-23038.010043/2013-02]

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This study investigated the protein content of the hydatid fluid compartment in E. granulosus and E. ortleppi pulmonary bovine cysts and compared their molecular arsenal at the host-parasite interface. The results showed a predominance of parasite proteins compared to host proteins in the hydatid fluid samples. Functional analysis revealed important molecular functions and processes that are active in pulmonary cystic echinococcosis.
Background: Most cystic echinococcosis cases in Southern Brazil are caused by Echinococcus granulosus and Echinococcus ortleppi. Proteomic studies of helminths have increased our knowledge about the molecular survival strategies that are used by parasites. Here, we surveyed the protein content of the hydatid fluid compartment in E. granulosus and E. ortleppi pulmonary bovine cysts to better describe and compare their molecular arsenal at the host-parasite interface. Methods: Hydatid fluid samples from three isolates of each species were analyzed using mass spectrometry-based proteomics (LC-MS/MS). In silico functional analyses of the identified proteins were performed to examine parasite survival strategies. Results: The identified hydatid fluid protein profiles showed a predominance of parasite proteins compared to host proteins that infiltrate the cysts. We identified 280 parasitic proteins from E. granulosus and 251 from E. ortleppi, including 52 parasitic proteins that were common to all hydatid fluid samples. The in silico functional analysis revealed important molecular functions and processes that are active in pulmonary cystic echinococcosis, such as adhesion, extracellular structures organization, development regulation, signaling transduction, and enzyme activity. Conclusions: The protein profiles described here provide evidence of important mechanisms related to basic cellular processes and functions that act at the host-parasite interface in cystic echinococcosis. The molecular tools used by E. granulosus and E. ortleppi for survival within the host are potential targets for new therapeutic approaches to treat cystic echinococcosis and other larval cestodiases.

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