Cryptosporidium parvum contains a unique fusion protein pyruvate:NADP+ oxidoreductase (CpPNO) that is composed of two distinct, conserved domains, an N-terminal pyruvate:ferredoxin oxidoreductase (PFO) and a C-terminal cytochrome P450 reductase (CPR). Unlike a similar fusion protein that localizes to the mitochondrion of the photosynthetic protist Euglena gracilis, CpPNO lacks an N-terminal mitochondrial targeting sequence. Using two distinct polyclonal antibodies raised against CpPFO and one polyclonal antibody against CpCPR, Western blot analysis has shown that sporozoites of C. parvum express the entire CpPNO fusion protein. Furthermore, confocal immunofluorescence and transmission electron microscopy confirm that CpPNO is localized within the cytosol rather than the relict mitochondrion of C. parvum. The distribution of this protein is not, however, strictly confined to the cytosol. CpPNO also appears to localize posteriorly within the crystalloid body.

• MeSH
• Cryptosporidium parvum cytologie   enzymologie   genetika   MeSH
• cytosol enzymologie   MeSH
• Euglena gracilis cytologie   enzymologie   MeSH
• financování organizované MeSH
• fluorescenční mikroskopie MeSH
• ketonoxidoreduktasy analýza   genetika   imunologie   MeSH
• konfokální mikroskopie MeSH
• NADPH-cytochrom c-reduktasa analýza   genetika   imunologie   MeSH
• organely enzymologie   MeSH
• protozoální proteiny analýza   MeSH
• pyruvátsynthasa analýza   genetika   imunologie   MeSH
• sporozoiti cytologie   enzymologie   MeSH
• transmisní elektronová mikroskopie MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH