A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum.

摘要: Abstract Recent studies suggest that peptidyl-prolyl isomerases of the cyclophilin family, access secretory pathway, can be involved in interaction parasitic protozoa with mammalian host cells. The amino acid sequence a cDNA encoding family member intracellular protozoan parasite cattle Theileria parva contains conserved C-terminal domain exhibits 70% identity to proteins from other organisms, and unique 60 novel N-terminal extension. Cell-free expression revealed 26 kDa translation product, indicating domain. protein-coding region three short introns, less than 100 base pairs length Northern blot analysis demonstrates single 0.9 kb transcript piroplasm schizont stages. is present high abundance intra-lymphocytic stage. recombinant protein binds immobilized cyclosporin A, finding consistent cis – trans isomerase function vivo. A predicted signal peptide was functional for entry into eukaryotic transport pathway cell-free vitro transcription/translation system. translocated across membrane endoplasmic reticulum uncleaved functioned as anchor.