Abstract
Cryptosporidium is a life-threating protozoan parasite belonging to the phylum Apicomplexa, which mainly causes gastroenteritis in a variety of vertebrate hosts. Currently, there is a re-emergence of Cryptosporidium infection; however, no fully effective drug or vaccine is available to treat Cryptosporidiosis. In the present study, to better understand the detailed interaction between the host and Cryptosporidium parvum, a large-scale label-free proteomics study was conducted to characterize the changes to the proteome induced by C. parvum infection. Among 4406 proteins identified, 121 proteins were identified as differentially abundant (> 1.5-fold cutoff, P < 0.05) in C. parvum infected HCT-8 cells compared with uninfected cells. Among them, 67 proteins were upregulated, and 54 proteins were downregulated at 36 h post infection. Analysis of the differentially abundant proteins revealed an interferon-centered immune response of the host cells against C. parvum infection and extensive inhibition of metabolism-related enzymes in the host cells caused by infection. Several proteins were further verified using quantitative real-time reverse transcription polymerase chain reaction and western blotting. This systematic analysis of the proteomics of C. parvum-infected HCT-8 cells identified a wide range of functional proteins that participate in host anti-parasite immunity or act as potential targets during infection, providing new insights into the molecular mechanism of C. parvum infection.
Highlights
Cryptosporidium is an opportunistic pathogen with a worldwide distribution, which infects a variety of vertebrates [1]
Cryptosporidium parvum is an emerging zoonotic pathogen transmitted via the fecal–oral route, and is considered a leading cause of moderate-to-severe diarrheal disease in young children in resource limited areas
Functional enrichment analysis indicated that the upregulated proteins were concentrated in the transporters associated with antigen processing (TAP) complex, extracellular space, intrinsic component of plasma membrane, and MHC class I peptide loading complex
Summary
Cryptosporidium is an opportunistic pathogen with a worldwide distribution, which infects a variety of vertebrates (including humans, mammals, reptiles, amphibians, and poultry) [1]. Immunocompetent individuals experience a self-limiting illness after C. parvum infection; immunocompromised hosts suffer from more severe and prolonged gastrointestinal disease that can be fatal [2,3]. Cryptosporidium parasitizes mainly the epithelial cells of the gastrointestinal and respiratory tracts, evoking host epithelial defense responses mediated by Toll like receptors (TLRs) [5,6,7,8]. In contrast to other apicomplexans, such as Toxoplasma gondii and Plasmodium falciparum, Cryptosporidium has lost the plastid and mitochondrial genomes, and both the asexual and sexual stages are completed within a single host [9,10,11]. Cryptosporidium metabolism is almost exclusively based on glycolysis, which is likely to be the reason why it parasitizes mainly gut epithelial cells [9,10]. C. parvum does not fully invade the host cell, but resides intracellularly in the parasitophorous vacuole with an epicellular location
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