Glycolytic enzyme activities in Cryptosporidium parvum oocysts

Entrala, Emilio; Mascaró, C.

doi:10.1016/s0378-1097(97)00136-5

Cited by 18 publications

(14 citation statements)

References 15 publications

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“…Notably, metabolic enzymes such as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase and protein di-sulphide isomerase were also recorded. This is consistent with the hypothesis that glycolysis might be the sole energy source of C. parvum and that the parasite primarily relies on the anaerobic oxidation of glucose for energy production [1-3,5,18]. In addition, no enzymes of the TCA cycle or cytochrome respiratory pathways were revealed during this study.…”

Section: Discussionsupporting

confidence: 91%

Sporozoite proteome analysis ofCryptosporidium parvumby one-dimensional SDS-PAGE and liquid chromatography tandem mass spectrometry

Siddiki

2013

J Vet Sci

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Despite the development of new technologies, new challenges still remain for large scale proteomic profiling when dealing with complex biological mixtures. Fractionation prior to liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis is usually the preferred method to reduce the complexity of any biological sample. In this study, a gel LC-MS/MS approach was used to explore the stage specific proteome of Cryptosporidium (C.) parvum. To accomplish this, the sporozoite protein of C. parvum was first fractionated using SDS-PAGE with subsequent LC-MS/MS analysis. A total of 135 protein hits were recorded from 20 gel slices (from same gel lane), with many hits occurring in more than one band. Excluding all non-Cryptosporidium entries and proteins with multiple hits, 33 separate C. parvum entries were identified during the study. The overall goal of this study was to reduce sample complexity by protein fractionation and increase the possibility of detecting proteins present in lower abundance in a complex protein mixture.

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Section: Discussionsupporting

confidence: 91%

Sporozoite proteome analysis ofCryptosporidium parvumby one-dimensional SDS-PAGE and liquid chromatography tandem mass spectrometry

Siddiki

2013

J Vet Sci

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“…In extracellular sporozoites and merozoites, Cp LDH has been shown to be localised in the cytosol ( Zhang et al, 2015 ), implying that it is important for generation of parasite energy during these stages and would, therefore, be important during the host cell invasion process. Indeed, proteomic and genomic analyses of Cryptosporidium have indicated that glycolysis is the sole energy source in Cryptosporidium ( Entrala and Mascaró, 1997 , Xu et al, 2004 , Siddiki, 2013 ), which is consistent with our findings that Cp LDH is essential for growth, propagation and viability of C. parvum in vivo.…”

Section: Discussionsupporting

confidence: 92%

Morpholino-mediated in vivo silencing of Cryptosporidium parvum lactate dehydrogenase decreases oocyst shedding and infectivity

Zhang

Kim

Worthen

et al. 2018

International Journal for Parasitology

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“…Because there are no typical eukaryotic N‐terminal targeting presequences on either CpLDHl or CpMDHl (Fig. 1, Lines 1 and 2), the data also strongly suggest that these enzymes are cytosolic rather than organellar, and that they are probably responsible for the LDH and MDH activities described earlier in the cytosolic fraction of C. parvum oocysts (Entrala and Mascaro 1997). The unique insertion of 5 amino acids within the active site loop (Simmons et al 1985; Yang and Parmley 1997) seen in T. gondii and P. falciparum LDH is also absent from CpLDHl and CpMDHl (Fig.…”

Section: Resultsmentioning

confidence: 70%

α‐Proteobacterial Relationship of Apicomplexan Lactate and Malate Dehydrogenases

Zhu

Keithly

2002

J Eukaryotic Microbiology

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We have cloned and sequenced a lactate dehydrogenase (LDH) gene from Cryptosporidium parvum (CpLDH1). With this addition, and that of four recently deposited alpha-proteobacterial malate dehydrogenase (MDH) genes, the phylogenetic relationships among apicomplexan LDH and bacterial MDH were re-examined. Consistent with previous studies, our maximum likelihood (ML) analysis using the quartet-puzzling method divided 105 LDH/MDH enzymes into five clades, and confirmed that mitochondrial MDH is a sister clade to those of y-proteobacteria, rather than to alpha-proteobacteria. In addition, a Cryptosporidium parvum MDH (CpMDH1) was identified from the ongoing Cryptosporidium genome project that appears to belong to a distinct clade (III) comprised of 22 sequences from one archaebacterium, numerous eubacteria, and several apicomplexans. Using the ML puzzling test and bootstrapping analysis with protein distance and parsimony methods, the resulting trees not only robustly confirmed the alpha-proteobacterial relationship of apicomplexan LDH/MDH, but also supported a monophyletic relationship of CpLDH1 with CpMDHI. These data suggest that, unlike most other eukaryotes, the Apicomplexa may be one of the few lineages retaining an alpha-proteobacterial-type MDH that could have been acquired from an ancestral alpha-proteobacterium through primary endosymbiosis giving rise to the mitochondria, or through an unknown lateral gene transfer (LGT) event.

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Glycolytic enzyme activities in Cryptosporidium parvum oocysts

Cited by 18 publications

References 15 publications

Sporozoite proteome analysis ofCryptosporidium parvumby one-dimensional SDS-PAGE and liquid chromatography tandem mass spectrometry

Sporozoite proteome analysis ofCryptosporidium parvumby one-dimensional SDS-PAGE and liquid chromatography tandem mass spectrometry

Morpholino-mediated in vivo silencing of Cryptosporidium parvum lactate dehydrogenase decreases oocyst shedding and infectivity

α‐Proteobacterial Relationship of Apicomplexan Lactate and Malate Dehydrogenases

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