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Acanthamoeba castellanii: Proteins involved in actin dynamics, glycolysis, and proteolysis are regulated during encystation
- Source :
- Experimental Parasitology. 123:90-94
- Publication Year :
- 2009
- Publisher :
- Elsevier BV, 2009.
-
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.
- Subjects :
- Proteolysis
Immunology
Protozoan Proteins
Fructose-bisphosphate aldolase
DNA-binding protein
Mass Spectrometry
Fructose-Bisphosphate Aldolase
parasitic diseases
medicine
Animals
Electrophoresis, Gel, Two-Dimensional
Actin
Gel electrophoresis
Serine protease
Acanthamoeba castellanii
biology
medicine.diagnostic_test
Microfilament Proteins
Serine Endopeptidases
General Medicine
Actins
Cell biology
Infectious Diseases
Biochemistry
Phosphopyruvate Hydratase
Proteome
biology.protein
Parasitology
Glycolysis
Subjects
Details
- ISSN :
- 00144894
- Volume :
- 123
- Database :
- OpenAIRE
- Journal :
- Experimental Parasitology
- Accession number :
- edsair.doi.dedup.....6828b3bded9eeaaddecad9841caea32b
- Full Text :
- https://doi.org/10.1016/j.exppara.2009.06.006