title: Differential Gene Expression and Protein Localization of Cryptosporidium parvum Fatty Acyl-CoA Synthetase Isoforms.
abstract: Cryptosporidium parvum is unable to synthesize fatty acids de novo, but possesses three long-chain fatty acyl-CoA synthetase (CpACS) isoforms for activating fatty acids. We have recently shown that these enzymes could be targeted to kill the parasite in vitro and in vivo. Here, we demonstrated that the CpACS genes were differentially expressed during the parasite life cycle, and their proteins were localized to different subcellular structures by immunofluorescence and immuno-electron microscopies. Among them, CpACS1 displayed as an apical protein in sporozoites and merozoites, but no or little presence during the intracellular merogony until the release of merozoites, suggesting that CpACS1 probably functioned mainly during the parasite invasion and/or early stage of intracellular development. Both CpACS2 and CpACS3 proteins were present in all parasite life cycle stages, in which CpACS2 was present in the parasite and the parasitophorous vacuole membranes (PVM), whereas CpACS3 was mainly present in the parasite plasma membranes with little presence in the PVM. These observations suggest that CpACS2 and CpACS3 may participate in scavenging and transport of fatty acids across the PVM and the parasite cytoplasmic membranes, respectively.
authors.affiliation: Department of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas.
authors.forename: Fengguang
authors.initials: F
authors.lastname: Guo
authors.affiliation: Department of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas.
authors.forename: Haili
authors.initials: H
authors.lastname: Zhang
authors.affiliation: Department of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas.
authors.forename: Harold Ross
authors.initials: HR
authors.lastname: Payne
authors.affiliation: Department of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas.
authors.forename: Guan
authors.initials: G
authors.lastname: Zhu
mesh_terms: D000214:Acyl Coenzyme A / Q000235:genetics / Q000378:metabolism; D003066:Coenzyme A Ligases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism*; D016785:Cryptosporidium parvum / Q000166:cytology / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic; D007527:Isoenzymes; D008018:Life Cycle Stages / Q000502:physiology; D052940:Merozoites / Q000378:metabolism; D010802:Phylogeny; D021381:Protein Transport; D015800:Protozoan Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D012337:RNA, Ribosomal, 18S / Q000235:genetics; D034101:Sporozoites / Q000378:metabolism
chemical_list: D000214:Acyl Coenzyme A; D005227:Fatty Acids; D007527:Isoenzymes; D015800:Protozoan Proteins; D012337:RNA, Ribosomal, 18S; D003066:Coenzyme A Ligases
keywords: Apical proteins; Apicomplexa; enzyme; fatty acid activation; immuno-electron microscopy; immunofluorescence microscopy; parasitophorous vacuole membrane