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Localization of pyruvate:NADP+ oxidoreductase in sporozoites of Cryptosporidium parvum
Ctrnacta V, Ault JG, Stejskal F, Keithly JS.
Jazyk angličtina Země Spojené státy americké
NLK
Medline Complete (EBSCOhost)
od 2004-09-01 do Před 1 rokem
Wiley Online Library (archiv)
od 1997-01-01 do 2012-12-31
- 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
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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- 314 __
- $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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