Acanthamoeba castellanii: proteins involved in actin dynamics, glycolysis, and proteolysis are regulated during encystation

Exp Parasitol. 2009 Sep;123(1):90-4. doi: 10.1016/j.exppara.2009.06.006. Epub 2009 Jun 10.

Abstract

Acanthamoeba castellanii is a pathogenic free-living amoeba. Cyst forms are particularly important in their pathogenicity, as they are more resistant to treatments and might protect pathogenic intracellular bacteria. However, encystation is poorly understood at the molecular level and global changes at the protein level have not been completely described. In this study, we performed two-dimensional gel electrophoresis to compare protein expression in trophozoite and cyst forms. Four proteins, specifically expressed in trophozoites, and four proteins, specifically expressed in cysts, were identified. Two proteins, enolase and fructose bisphosphate aldolase, are involved in the glycolytic pathway. Three proteins are likely actin-binding proteins, which is consistent with the dramatic morphological modifications of the cells during encystation. One protein belongs to the serine protease family and has been already linked to encystation in A. castellanii. In conclusion, this study found that the proteins whose expression was modified during encystation were likely involved in actin dynamics, glycolysis, and proteolysis.

MeSH terms

  • Acanthamoeba castellanii / pathogenicity
  • Acanthamoeba castellanii / physiology*
  • Actins / metabolism*
  • Animals
  • Electrophoresis, Gel, Two-Dimensional
  • Fructose-Bisphosphate Aldolase / metabolism
  • Glycolysis
  • Mass Spectrometry
  • Microfilament Proteins / metabolism
  • Phosphopyruvate Hydratase / metabolism
  • Protozoan Proteins / metabolism
  • Protozoan Proteins / physiology*
  • Serine Endopeptidases / metabolism

Substances

  • Actins
  • Microfilament Proteins
  • Protozoan Proteins
  • Serine Endopeptidases
  • Fructose-Bisphosphate Aldolase
  • Phosphopyruvate Hydratase