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dc.contributor.authorEbel, T.
dc.contributor.authorPelle, Roger
dc.contributor.authorJanoo, R.T.K.
dc.contributor.authorLipp, J.
dc.contributor.authorBishop, Richard P.
dc.date.accessioned2013-07-03T05:26:16Z
dc.date.available2013-07-03T05:26:16Z
dc.date.issued2004
dc.identifier.citationVeterinary Parasitology;121(1-2): 65-77
dc.identifier.issn0304-4017
dc.identifier.urihttp://hdl.handle.net/10568/33235
dc.description.abstractRecent 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.
dc.language.isoen
dc.sourceVeterinary Parasitology
dc.subjectTHEILERIA PARVA
dc.subjectCELLS
dc.subjectNUCLEOTIDE SEQUENCE
dc.subjectPEPTIDES
dc.subjectENDOPLASMIC RETICULUM
dc.titleA membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum
dc.typeJournal Article
cg.subject.ilriANIMAL DISEASES
cg.subject.ilriLIVESTOCK
cg.identifier.statusLimited Access
cg.identifier.doihttps://dx.doi.org/10.1016/j.vetpar.2004.02.007


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