4.2 Article

Echinococcus multilocularis: Proteomic analysis of the protoscoleces by two-dimensional electrophoresis and mass spectrometry

Journal

EXPERIMENTAL PARASITOLOGY
Volume 123, Issue 2, Pages 162-167

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.exppara.2009.06.014

Keywords

Echinococcus multilocularis; Protoscolex; Two-dimensional electrophoresis; Proteomics; Mass spectrometry; Immunoproteomics; Vaccine

Categories

Funding

  1. Natural Science Fund of China [30471514]
  2. Program for New Century Excellent Talents in Fujian Province University
  3. Project of Innovation Foundation of Xiamen University

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Echinococcus multilocularis is an important parasite that causes human alveolar echinococcosis. Identification and characterization of the proteins encoded by E. multilocularis metacestode might help to understand the complexity of the parasites and their interactions with the host, and to identify new candidates for immunodiagnosis and vaccine development. Here we present a proteomic analysis of E. multilocularis protoscolex (PSC) proteins. The proteins were resolved by 2-DE (pH range 3.5-10), followed by MALDI-TOF MS analysis. Fourteen known Echinococcus proteins were identified, including cytoskeletal proteins, heat shock proteins, metabolic enzymes, 14-3-3 protein, antigen P-29 and calreticulin. To construct a systematic reference map of the immunogenic proteins from E. multilocularis PSC, immunoblot analysis of PSC 2-DE maps was performed. Over 50 proteins spots were detected on immunoblots as antigens and 15 of them were defined. The results showed that cytoskeletal proteins and heat shock proteins were immunodominant antigens in alveolar echinococcosis. (C) 2009 Elsevier Inc. All rights reserved.

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