Short Communication

Proteomic analysis of the larval stage of the parasite Echinococcus granulosus: Causative agent of cystic hydatid disease

  1. Gustavo Chemale1,
  2. Arjan J. van Rossum2,
  3. James R. Jefferies,
  4. John Barrett2,
  5. Peter M. Brophy2,
  6. Henrique B. Ferreira1,
  7. Arnaldo Zaha1,*

Article first published online: 12 AUG 2003

DOI: 10.1002/pmic.200300487

Issue

PROTEOMICS

PROTEOMICS

Special Issue: SPS Proceedings 2nd Annual Congress Lausanne, 3–5 December 2002

Volume 3, Issue 8, pages 1633–1636, August 2003

Additional Information

How to Cite

Chemale, G., van Rossum, A. J., Jefferies, J. R., Barrett, J., Brophy, P. M., Ferreira, H. B. and Zaha, A. (2003), Proteomic analysis of the larval stage of the parasite Echinococcus granulosus: Causative agent of cystic hydatid disease. Proteomics, 3: 1633–1636. doi: 10.1002/pmic.200300487

Author Information

  1. 1

    Centro de Biotecnologia and Departamento de Biologia Molecular e Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil

  2. 2

    Institute of Biological Sciences, University of Wales, Aberystwyth, Wales

*Centro de Biotecnologia and Departamento de Biologia Molecular e Biotecnologia, Universidade Federal do Rio Grande do Sul, Caixa Postal 15005, Porto Alegre, 91501-970, RS, Brazil Fax: +55-51-33167309

Publication History

  1. Issue published online: 12 AUG 2003
  2. Article first published online: 12 AUG 2003
  3. Manuscript Received: 2 JUL 2002

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Keywords:

  • Actin;
  • Echinococcus granulosus;
  • Heat shock protein;
  • Trichloracetic acid precipitation;
  • Two-dimensional gel electrophoresis

Abstract

We describe the preparation of Echinococcus granulosus metacestode protein extracts for two-dimensional electrophoresis (2-DE). Protoscoleces and hydatid fluid were prepared by precipitation using trichloroacetic acid (TCA) to remove nonprotein contaminants. Compared to the untreated control, TCA precipitation improved the 2-DE gel profile of the protoscoleces proteins. Comparison of 2-DE gels from insoluble and soluble fractions of the protoscoleces protein extract showed that most proteins are insoluble after lysis by sonication. Host serum proteins, especially albumin and globulins, caused horizontal streaking problems on the hydatid fluid 2-DE gels due to their high content in this sample. Even after the preparation of a hydatid fluid parasite enriched fraction, the high amount of bovine serum albumin and globulins made parasite-specific proteins difficult to detect by 2-DE. Despite the absence of an E. granulosus genome sequencing or expressed sequence tag (EST) projects, it was possible to identify 15 prominent protein spots from a whole protein protoscoleces 2-DE gel by peptide mass fingerprinting. These include actins, tropomyosin, paramyosin, thioredoxin reductase, antigen P-29, cyclophilin, and the heat shock proteins hsp70 and hsp20. This work demonstrates that 2-DE and PMF are important tools to identify proteins from the hydatid fluid and protoscoleces and for the comparative analysis of cysts from different hosts or between active and resting cysts.

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