Lifecycle progression and sexual development of the apicomplexan parasite Cryptosporidium parvum
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ABSTRACT:
PROVIDER: PRJNA530692 | ENA |
REPOSITORIES: ENA
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Project description:The apicomplexan parasite Cryptosporidium is a leading global cause of severe diarrheal disease and an important contributor to early childhood mortality. Currently there are no fully effective treatments or vaccines available. Transmission of the disease occurs through ingestion of oocysts, through direct contact or contaminated water or food. Oocysts are meiotic spores and the product of parasite sex. Cryptosporidium has a single host lifecycle where both asexual and sexual processes unfold in the intestine of infected hosts. Here we use the new-found ability to genetically engineer Cryptosporidium to make life cycle progression and parasite sex tractable. We derive reporter strains to follow parasite development in culture and infected mice and define the genes that orchestrate sex and oocyst formation through mRNA sequencing of sorted cells. After two days, parasites in cell culture show pronounced sexualization, but productive fertilization does not occur and infection falters. In contrast in infected mice, male gametes successfully fertilize females, leading to meiotic division and sporulation. To rigorously test for fertilization, we devised a two-component genetic crossing assay employing a Cre recombinase activated reporter. Our findings suggest obligate developmental progression towards sex in Cryptosporidium, which has important implications for the treatment and prevention of the infection.
2019-09-03 | GSE129267 | GEO
Project description:Cryptosporidium parvum is an important zoonotic parasitic disease worldwide, but the molecular mechanisms of the host–parasite interaction are not fully understood. Noncoding microRNAs (miRNAs) are considered key regulators of parasitic diseases. Therefore, we used microarray, qPCR, and bioinformatic analyses to investigate the intestinal epithelial miRNA expression profile after Cryptosporidium parvum infection.Twenty miRNAs were differentially expressed after infection (four upregulated and 16 downregulated). Further analysis of the differentially expressed miRNAs revealed that many important cellular responses were triggered by Cryptosporidium parvum infection, including cell apoptosis and the inflammatory and immune responses.This study demonstrates for the first time that the miRNA expression profile of human intestinal epithelium cells is altered by C. parvum infection. This dysregulation of miRNA expression may contribute to the regulation of host biological processes in response to C. parvum infection, including cell apoptosis and the immune responses. These results provide new insight into the regulatory mechanisms of host miRNAs during cryptosporidiosis, which may offer potential targets for future C. parvum control strategies.
2018-12-23 | GSE95365 | GEO
Project description:H69 cells were cultured in H69 medium with Cryptosporidium parvum oocysts(10 X 5 per well, for smaples 04, 05 and 06) or without oocysts(for samples 01, 02 and 03)for 8 hours and then collected for array analysis. Sample 07 was cells exposed to heated inactived oocysts. <br>
2010-02-11 | E-MEXP-2050 | biostudies-arrayexpress
Project description:Cryptosporidium parvum is a zoonotic apicomplexan parasite and a common cause of diarrheal disease worldwide. The development of vaccines to prevent or limit infection remains an important goal for tackling these diarrheal diseases, which are a significant cause of infant morbidity in the developing world. The only approved vaccine against an apicomplexan parasite targets conserved adhesins possessing a thrombospondin repeat (TSR) domains. Orthologous TSR domain-containing proteins are commonplace in the apicomplexa and C. parvum possess 12 such proteins. Here, we explore the molecular evolution and conservation of these proteins and examine their abundance in C. parvum oocysts to assess the likelihood that they may be useful as vaccine candidates. We go onto examine the glycosylation states of these proteins using antibody-enabled and ZIC-HILIC enrichment techniques, which revealed that these proteins are modified with C-linked Hex and N-linked Hex5-6HexNAc2 glycans.
2023-01-12 | PXD023935 | Pride
Project description:Cryptosporidium parvum is a zoonotic apicomplexan parasite and a common cause of diarrheal disease worldwide. The development of vaccines to prevent or limit infection remains an important goal for tackling these diarrheal diseases, which are a significant cause of infant morbidity in the developing world. The only approved vaccine against an apicomplexan parasite targets conserved adhesins possessing a thrombospondin repeat (TSR) domains. Orthologous TSR domain-containing proteins are commonplace in the apicomplexa and C. parvum possess 12 such proteins. Here, we explore the molecular evolution and conservation of these proteins and examine their abundance in C. parvum oocysts to assess the likelihood that they may be useful as vaccine candidates. We go onto examine the glycosylation states of these proteins using antibody-enabled and ZIC-HILIC enrichment techniques, which revealed that these proteins are modified with C-linked Hex and N-linked Hex5-6HexNAc2 glycans.
2023-01-12 | PXD023934 | Pride
Project description:Cryptosporidium parvum is a zoonotic apicomplexan parasite and a common cause of diarrheal disease worldwide. The development of vaccines to prevent or limit infection remains an important goal for tackling these diarrheal diseases, which are a significant cause of infant morbidity in the developing world. The only approved vaccine against an apicomplexan parasite targets conserved adhesins possessing a thrombospondin repeat (TSR) domains. Orthologous TSR domain-containing proteins are commonplace in the apicomplexa and C. parvum possess 12 such proteins. Here, we explore the molecular evolution and conservation of these proteins and examine their abundance in C. parvum oocysts to assess the likelihood that they may be useful as vaccine candidates. We go onto examine the glycosylation states of these proteins using antibody-enabled and ZIC-HILIC enrichment techniques, which revealed that these proteins are modified with C-linked Hex and N-linked Hex5-6HexNAc2 glycans.
2023-01-12 | PXD023936 | Pride
Project description:The Cryptosporidium parvum (C. parvum) oocyst wall provides strong protection against hostile environmental factors; however, research is limited concerning about the oocyst wall at the proteomic level. In this study, a comprehensive analysis of the proteome expressed by the oocyst wall of C. parvum was performed using label-free qualitative high-performance liquid chromatography (HPLC) fractionation and mass spectrometry-based qualitative proteomics technologies. A total of 798 proteins were identified, accounting for about 20% of the CryptoDB proteome. By using bioinformatic analysis, functional annotation and subcellular localization of the identified proteins were examined for better understanding of the characteristics of the oocyst wall. Among the identified proteins, one protein encoded by the C. parvum cgd7_5140 (Cpcgd7_5140) gene was predicted to be located on the surface of the oocyst wall. To verify its localization, an indirect immunofluorescent antibody assay (IFA) demonstrated that the Cpcgd7_5140 was localized on the surface of the oocyst wall, illustrating the potential usage as a marker for C. parvum detection in vitro. The results provide new information about the proteomic composition of the Cryptosporidium oocyst wall, thereby providing a theoretical basis for further study of Cryptosporidium oocyst wall formation as well as the selection of targets for Cryptosporidium detection.
2022-10-05 | PXD029431 | Pride