A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum
Recent studies suggest that peptidyl-prolyl isomerases of the cyclophilin family, that access the secretory pathway, can be involved in the interaction of parasitic protozoa with mammalian host cells. The amino acid sequence of a cDNA encoding a cyclophilin family member of the intracellular protozo...
| Autores principales: | , , , , |
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| Formato: | Journal Article |
| Lenguaje: | Inglés |
| Publicado: |
Elsevier
2004
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| Materias: | |
| Acceso en línea: | https://hdl.handle.net/10568/33235 |
| _version_ | 1855542390896459776 |
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| author | Ebel, T. Pelle, Roger Janoo, R.T.K. Lipp, J. Bishop, Richard P. |
| author_browse | Bishop, Richard P. Ebel, T. Janoo, R.T.K. Lipp, J. Pelle, Roger |
| author_facet | Ebel, T. Pelle, Roger Janoo, R.T.K. Lipp, J. Bishop, Richard P. |
| author_sort | Ebel, T. |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | Recent studies suggest that peptidyl-prolyl isomerases of the cyclophilin family, that access the secretory pathway, can be involved in the interaction of parasitic protozoa with mammalian host cells. The amino acid sequence of a cDNA encoding a cyclophilin family member of the intracellular protozoan parasite of cattle Theileria parva contains a conserved C-terminal domain that exhibits 70% amino acid identity to cyclophilin proteins from other organisms, and a unique 60 amino acid novel N-terminal extension. Cell-free expression of the cDNA revealed a 26kDa amino translation product, indicating expression of the N-terminal domain. The protein-coding region contains three short introns, less than 100 base pairs in length and Northern blot analysis demonstrates expression of a single 0.9kb transcript in the piroplasm and schizont stages. The transcript is present in high abundance in the intra-lymphocytic schizont stage. The recombinant protein binds to immobilized cyclosporin A, a finding consistent with peptidyl-prolyl cis-trans isomerase function in vivo. A predicted N-terminal signal peptide was functional for entry into the eukaryotic secretory transport pathway in a cell-free in vitro transcription/translation system. The C-terminal cyclophilin domain was translocated across the membrane of the endoplasmic reticulum and the uncleaved signal peptide functioned as a membrane anchor. |
| format | Journal Article |
| id | CGSpace33235 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 2004 |
| publishDateRange | 2004 |
| publishDateSort | 2004 |
| publisher | Elsevier |
| publisherStr | Elsevier |
| record_format | dspace |
| spelling | CGSpace332352024-05-01T08:20:00Z A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum Ebel, T. Pelle, Roger Janoo, R.T.K. Lipp, J. Bishop, Richard P. theileria parva cells nucleotide sequence peptides endoplasmic reticulum Recent studies suggest that peptidyl-prolyl isomerases of the cyclophilin family, that access the secretory pathway, can be involved in the interaction of parasitic protozoa with mammalian host cells. The amino acid sequence of a cDNA encoding a cyclophilin family member of the intracellular protozoan parasite of cattle Theileria parva contains a conserved C-terminal domain that exhibits 70% amino acid identity to cyclophilin proteins from other organisms, and a unique 60 amino acid novel N-terminal extension. Cell-free expression of the cDNA revealed a 26kDa amino translation product, indicating expression of the N-terminal domain. The protein-coding region contains three short introns, less than 100 base pairs in length and Northern blot analysis demonstrates expression of a single 0.9kb transcript in the piroplasm and schizont stages. The transcript is present in high abundance in the intra-lymphocytic schizont stage. The recombinant protein binds to immobilized cyclosporin A, a finding consistent with peptidyl-prolyl cis-trans isomerase function in vivo. A predicted N-terminal signal peptide was functional for entry into the eukaryotic secretory transport pathway in a cell-free in vitro transcription/translation system. The C-terminal cyclophilin domain was translocated across the membrane of the endoplasmic reticulum and the uncleaved signal peptide functioned as a membrane anchor. 2004-05 2013-07-03T05:26:16Z 2013-07-03T05:26:16Z Journal Article https://hdl.handle.net/10568/33235 en Limited Access Elsevier Veterinary Parasitology;121(1-2): 65-77 |
| spellingShingle | theileria parva cells nucleotide sequence peptides endoplasmic reticulum Ebel, T. Pelle, Roger Janoo, R.T.K. Lipp, J. Bishop, Richard P. A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum |
| title | A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum |
| title_full | A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum |
| title_fullStr | A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum |
| title_full_unstemmed | A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum |
| title_short | A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum |
| title_sort | membrane anchored theileria parva cyclophilin with a non cleaved amino terminal signal peptide for entry into the endoplasmic reticulum |
| topic | theileria parva cells nucleotide sequence peptides endoplasmic reticulum |
| url | https://hdl.handle.net/10568/33235 |
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