title: Acanthamoeba castellanii: proteins involved in actin dynamics, glycolysis, and proteolysis are regulated during encystation.
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.
authors.affiliation: Laboratoire de Chimie et Microbiologie de l'Eau, UMR CNRS 6008, Université de Poitiers, 86022 Poitiers Cedex, France.
authors.forename: Sabrina
authors.initials: S
authors.lastname: Bouyer
authors.forename: Marie-Hélène
authors.initials: MH
authors.lastname: Rodier
authors.forename: Alain
authors.initials: A
authors.lastname: Guillot
authors.forename: Yann
authors.initials: Y
authors.lastname: Héchard
mesh_terms: D048248:Acanthamoeba castellanii / Q000472:pathogenicity / Q000502:physiology*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D006019:Glycolysis; D013058:Mass Spectrometry; D008840:Microfilament Proteins / Q000378:metabolism; D010751:Phosphopyruvate Hydratase / Q000378:metabolism; D015800:Protozoan Proteins / Q000378:metabolism / Q000502:physiology*; D012697:Serine Endopeptidases / Q000378:metabolism
chemical_list: D000199:Actins; D008840:Microfilament Proteins; D015800:Protozoan Proteins; D012697:Serine Endopeptidases; D005634:Fructose-Bisphosphate Aldolase; D010751:Phosphopyruvate Hydratase