ArticleThe Journal of eukaryotic microbiology
Differential Gene Expression and Protein Localization of Cryptosporidium parvum Fatty Acyl-CoA Synthetase Isoforms.
Article in The Journal of eukaryotic microbiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Functional Characterization and Inhibition Analysis of a Glutathione Transferase fromPharmaceuticals (Basel, Switzerland) · 2026Article
- Article
- Molecular pathogenesis of Cryptosporidium and advancements in therapeutic interventions.Parasite (Paris, France) · 2025Review
- The acyl-CoA synthetasemBio · 2024Article
- Genetic diversity of Cryptosporidium spp., Encephalitozoon spp. and Enterocytozoon bieneusi in feral and captive pigeons in Central Europe.Parasitology research · 2024Article
- A single-pass type I membrane protein, mannose-specific L-type lectin, potentially involved in the adhesion and invasion of Cryptosporidium parvum.Parasite (Paris, France) · 2024Article
- Functional characterization of CpADF, an actin depolymerizing factor protein in Cryptosporidium parvum.Parasitology research · 2023Article
- The mucin-like, secretory type-I transmembrane glycoprotein GP900 in the apicomplexan Cryptosporidium parvum is cleaved in the secretory pathway and likely plays a lubrication role.Parasites & vectors · 2022Article
- Implication of Potential Differential Roles of the Two Phosphoglucomutase Isoforms in the Protozoan ParasitePathogens (Basel, Switzerland) · 2021Article
- Pantothenate and CoA biosynthesis in Apicomplexa and their promise as antiparasitic drug targets.PLoS pathogens · 2021Review
- Unique Tubulin-Based Structures in the Zoonotic Apicomplexan ParasiteMicroorganisms · 2021Article
- A Single-Pass Type I Membrane Protein from the Apicomplexan ParasiteMicroorganisms · 2021Article
- Gregarine single-cell transcriptomics reveals differential mitochondrial remodeling and adaptation in apicomplexans.BMC biology · 2021Article
- Discovery of New Microneme Proteins inFrontiers in veterinary science · 2021Article
- Article
- Molecular and Biochemical Characterization of a Type II Thioesterase From the Zoonotic Protozoan ParasiteFrontiers in cellular and infection microbiology · 2019Article
- NMR metabolomics reveals effects ofGut pathogens · 2019Article
- Preliminary Characterization of MEDLE-2, a Protein Potentially Involved in the Invasion ofFrontiers in microbiology · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
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