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Fibrillarin RNA methylase is an interacting protein of Cryptosporidium parvum calmodulin-like protein (CpCML).
- Source :
-
Microbial pathogenesis [Microb Pathog] 2022 Sep; Vol. 170, pp. 105679. Date of Electronic Publication: 2022 Jul 16. - Publication Year :
- 2022
-
Abstract
- Cryptosporidium parvum is an obligate protozoan parasite invading epithelial cells of small intestine of human and animals, and causing diarrheal disease. In apicomplexan parasites, calcium signaling can regulate many essential biological processes such as invasion and migration. As the main intracellular receptor for calcium ions, calmodulins control the activities of hundreds of enzymes and proteins. Calmodulin-like protein (CML) is an important member of the calmodulin family and may play a key role in C. parvum, however, the actual situation is still not clear. The present study aimed to identify the parasite interaction partner proteins of C. parvum calmodulin-like protein (CpCML). By constructing the cpcml bait plasmid, 5 potential CpCML - interacting proteins in C. parvum oocyst were screened by yeast-two-hybrid system (Y2H). Bimolecular fluorescence complementation (BiFC) and Co-immunoprecipitation (Co-IP) were performed as subsequent validations. Fibrillarin RNA methylase (FBL) was identified via this screening method as CpCML interacting protein in C. parvum. The identification of this interaction made it possible to get a further understanding of the function of CpCML and its contribution to the pathogenicity of C. parvum.<br />Competing Interests: Declaration of competing interest The authors have no conflicts of interest to declare.<br /> (Copyright © 2022 Elsevier Ltd. All rights reserved.)
- Subjects :
- Animals
Calmodulin genetics
Calmodulin metabolism
Chromosomal Proteins, Non-Histone
Humans
Protozoan Proteins genetics
Protozoan Proteins metabolism
tRNA Methyltransferases
Cryptosporidiosis parasitology
Cryptosporidium genetics
Cryptosporidium parvum genetics
Cryptosporidium parvum metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1096-1208
- Volume :
- 170
- Database :
- MEDLINE
- Journal :
- Microbial pathogenesis
- Publication Type :
- Academic Journal
- Accession number :
- 35843442
- Full Text :
- https://doi.org/10.1016/j.micpath.2022.105679