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Localization of pyruvate:NADP+ oxidoreductase in sporozoites of Cryptosporidium parvum
Ctrnacta V, Ault JG, Stejskal F, Keithly JS.
Language English Country United States
NLK
Medline Complete (EBSCOhost)
from 2004-09-01 to 1 year ago
Wiley Online Library (archiv)
from 1997-01-01 to 2012-12-31
- 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
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.
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- $a Department of Tropical Medicine, 1st Faculty of Medicine, Charles University, Prague, Czech Republic. vlastaxiv@hotmail.com
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- $a 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.
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