Dataset Information

A lysosomal hydrolase receptor, CPBF2, involve in invasion machinery of an enteric protozoan parasite Entamoeba histolytica

ABSTRACT: To know the role of lysosomal hydrolase receptors in virulecne of enteric protozoan parasite Entamoeba histolytica, eleven cysteine protease binding protein family (CPBF) proteins were specifically silenced and examined the effect on virulence-related phenotypes. Among them, CPBF2 gene silence caused defect in Matrigel invasion. To clarify transcriptomic difference in CPBF2 gene silenceing strain, RNA-seq analysis was conducted.

ORGANISM(S): Entamoeba histolytica

PROVIDER: GSE145637 | GEO | 2020/05/31

REPOSITORIES: GEO

ACCESS DATA

Similar Datasets

Project description:Characterization of the human microbiota is providing new insightsinto the complexity of host–parasite–bacterium relationships. Amoebiasis (an intestinal infection affecting a large proportion of the population in many countries worldwide) is caused by the amoebic parasite Entamoeba histolytica. During amoebiasis, the parasite encounters several types of stress as a result of the host’s response to infection. Given that E. histolytica phagocytises bacteria in the intestinal lumen, we hypothesized that enteric bacteria can influence the course of an amoebic infection. Hence, we used live Escherichia coli O55 as a pertinent model of the bacterial community’s contribution to amoebic responses during host- induced stress. By measuring amoebic survival, we found that live E. coli protected E. histolytica against oxidative stress (OS) but not against nitrosative stress. E. coli– associated protection is correlated with massive transcriptionalchanges in amoebic genes acquired through lateral transfer from the bacterial kingdom, including genes coding for proteinscontaining leucine-rich repeat (LRR) motifs. The transcriptome profile triggered by OS and E. coli was also observed with other enteric bacteria, including pathogens and non-pathogens. In contrast, exposure to a probiotic resulted in a different transcriptome profile. The present study shows that OS and live bacteria together modulate 84 of E. histolytica’s 137 LRR protein genes. The LRR proteins are involvedin protein-ligand and protein-protein interactions – especially in proteins that interact with bacteria as part of the innate immune response in mammals and plants, such as Toll-like receptors. The structural and functional homology of LRRs and TLRs identified here suggest that despite its old age in evolutionary terms, the protozoan E. histolytica displays key characteristics of higher eukaryotes’ innate immune systems. We conclude that components of innate immunity existed in the common ancestor of plants and animals

Dataset Information

A lysosomal hydrolase receptor, CPBF2, involve in invasion machinery of an enteric protozoan parasite Entamoeba histolytica

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure