Localization of pyruvate:NADP+ oxidoreductase in sporozoites of Cryptosporidium parvum
Language English Country United States Media print
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
Grant support
1R03 TW01507-01
FIC NIH HHS - United States
5D43 TW00915-05
FIC NIH HHS - United States
PubMed
16872290
DOI
10.1111/j.1550-7408.2006.00099.x
PII: JEU99
Knihovny.cz E-resources
- MeSH
- Cryptosporidium parvum cytology enzymology genetics growth & development MeSH
- Cytosol enzymology MeSH
- Euglena gracilis cytology enzymology 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 genetics MeSH
- Microscopy, Electron, Transmission MeSH
- Blotting, Western MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
- Names of Substances
- Ketone Oxidoreductases MeSH
- NADPH-Ferrihemoprotein Reductase MeSH
- Protozoan Proteins MeSH
- pyruvate dehydrogenase (NADP+) MeSH Browser
- Pyruvate Synthase 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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