Cryptosporidiosis

Chen, Xianming; Keithly, Janet S.; Payá, Carlos V.; LaRusso, Nicholas F.

doi:10.1056/nejmra013170

Cited by 461 publications

(411 citation statements)

References 48 publications

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“…Instead, this parasite is extracytoplasmic, covered by PVM on the surface of intestinal epithelial cells (Chen et al, 2002). Therefore, the PVM is the only barrier separating parasites from the intestinal lumen.…”

Section: Discussionmentioning

confidence: 99%

Functional characterization of a fatty acyl-CoA-binding protein (ACBP) from the apicomplexan Cryptosporidium parvum

2006

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In this paper, the identification and functional analysis of a fatty acyl-CoA-binding protein (ACBP) gene from the opportunistic protist Cryptosporidium parvum are described. The CpACBP1 gene encodes a protein of 268 aa that is three times larger than typical ACBPs (i.e. ∼90 aa) of humans and animals. Sequence analysis indicated that the CpACBP1 protein consists of an N-terminal ACBP domain (∼90 aa) and a C-terminal ankyrin repeat sequence (∼170 aa). The entire CpACBP1 ORF was engineered into a maltose-binding protein fusion system and expressed as a recombinant protein for functional analysis. Acyl-CoA-binding assays clearly revealed that the preferred binding substrate for CpACBP1 is palmitoyl-CoA. RT-PCR, Western blotting and immunolabelling analyses clearly showed that the CpACBP1 gene is mainly expressed during the intracellular developmental stages and that the level increases during parasite development. Immunofluorescence microscopy showed that CpACBP1 is associated with the parasitophorous vacuole membrane (PVM), which implies that this protein may be involved in lipid remodelling in the PVM, or in the transport of fatty acids across the membrane.

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Section: Discussionmentioning

confidence: 99%

Functional characterization of a fatty acyl-CoA-binding protein (ACBP) from the apicomplexan Cryptosporidium parvum

2006

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“…Although they have been reported in people from three days to 95 years old, the highest infection prevalence has been recognized in both children and young animals, and they are reported as a major cause of self-limiting diarrhea in immunocompetent people (Fayer et al, 1990;Chen et al, 2002). C. parvum is a particularly serious health threat to immunodeficient individuals, having no effective treatments for the disease (Kuczynska and Shelton 1999).…”

Section: Introductionmentioning

confidence: 99%

Risk factors associated with the occurrence of Cryptosporidium parvum infection in calves

Almeida¹,

Oliveira²,

Flores³

et al. 2010

Arq. Bras. Med. Vet. Zootec.

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Cryptosporidium parvum oocysts were detected in feces of dairy calves raised in Rio de Janeiro State and the risk factors involved in the infection were determined. A hundred calves aging up to 12-month-old from 13 dairy farms were sampled. Polymerase chain reaction was used to detect the presence of oocysts. The zoonotic C. parvum species was detected in 45% animals. Statistical risk factors analyses revealed an association between infection and animals raised in technical systems such as the use of milking equipment, milking cooler, and water trough (P<0.05).

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“…In AIDS patients, C. parvum is an opportunistic pathogen, causing significant morbidity and mortality by inducing chronic diarrhoeal disease (Chen et al, 2002). The lack of an effective therapy against human cryptosporidiosis has stimulated research on the basic biology of this parasite.…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial-type iron–sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum

et al. 2003

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Several reports have indicated that the iron-sulfur cluster [Fe-S] assembly machinery in most eukaryotes is confined to the mitochondria and chloroplasts. The best-characterized and most highly conserved [Fe-S] assembly proteins are a pyridoxal-59-phosphate-dependent cysteine desulfurase (IscS), and IscU, a protein functioning as a scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins. In this work, genes encoding IscS and IscU homologues have been isolated and characterized from the apicomplexan parasite Cryptosporidium parvum, an opportunistic pathogen in AIDS patients, for which no effective treatment is available. Primary sequence analysis (CpIscS and CpIscU) and phylogenetic studies (CpIscS) indicate that both genes are most closely related to mitochondrial homologues from other organisms. Moreover, the N-terminal signal sequences of CpIscS and CpIscU predicted in silico specifically target green fluorescent protein to the mitochondrial network of the yeast Saccharomyces cerevisiae. Overall, these findings suggest that the previously identified mitochondrial relict of C. parvum may have been retained by the parasite as an intracellular site for [Fe-S] assembly.

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Cryptosporidiosis

Cited by 461 publications

References 48 publications

Functional characterization of a fatty acyl-CoA-binding protein (ACBP) from the apicomplexan Cryptosporidium parvum

Functional characterization of a fatty acyl-CoA-binding protein (ACBP) from the apicomplexan Cryptosporidium parvum

Risk factors associated with the occurrence of Cryptosporidium parvum infection in calves

Mitochondrial-type iron–sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum

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