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 cytology   enzymology   genetics   MeSH
• Cytosol enzymology   MeSH
• Euglena gracilis cytology   enzymology   MeSH
• Financing, Organized MeSH
• Microscopy, Fluorescence MeSH
• Ketone Oxidoreductases analysis   genetics   immunology   MeSH
• Microscopy, Confocal MeSH
• NADPH-Ferrihemoprotein Reductase analysis   genetics   immunology   MeSH
• Organelles enzymology   MeSH
• Protozoan Proteins analysis   MeSH
• Pyruvate Synthase analysis   genetics   immunology   MeSH
• Sporozoites cytology   enzymology   MeSH
• Microscopy, Electron, Transmission MeSH
• Animals MeSH
• Check Tag
• Animals MeSH