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

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

PROVIDER: PRJNA607862 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11123413_1.fastq.gz	Fastqsanger.gz
	SRR11123413_2.fastq.gz	Fastqsanger.gz
	SRR11123414_1.fastq.gz	Fastqsanger.gz
	SRR11123414_2.fastq.gz	Fastqsanger.gz
	SRR11123415_1.fastq.gz	Fastqsanger.gz

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

Project description: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.

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Project description:Entamoeba histolytica is a protozoan parasite that causes colitis and liver abscesses. Several Entamoeba species and strains with differing levels of virulence have been identified. E. histolytica HM-1:IMSS is a virulent strain, E. histolytica Rahman is a nonvirulent strain, and Entamoeba dispar is a nonvirulent species. We used an E. histolytica DNA microarray consisting of 2,110 genes to assess the transcriptional differences between these species/strains with the goal of identifying genes whose expression correlated with a virulence phenotype. We found 415 genes expressed at lower levels in E. dispar and 32 genes with lower expression in E. histolytica Rahman than in E. histolytica HM-1:IMSS. Overall, 29 genes had decreased expression in both the nonvirulent species/strains than the virulent E. histolytica HM-1:IMSS. Interestingly, a number of genes with potential roles in stress response and virulence had decreased expression in either one or both nonvirulent Entamoeba species/strains. These included genes encoding Fe hydrogenase (9.m00419), peroxiredoxin (176.m00112), type A flavoprotein (6.m00467), lysozyme (6.m00454), sphingomyelinase C (29.m00231), and a hypothetical protein with homology to both a Plasmodium sporozoite threonine-asparagine-rich protein (STARP) and a streptococcal hemagglutinin (238.m00054). The function of these genes in Entamoeba and their specific roles in parasite virulence need to be determined. We also found that a number of the non-long-terminal-repeat retrotransposons (EhLINEs and EhSINEs), which have been shown to modulate gene expression and genomic evolution, had lower expression in the nonvirulent species/strains than in E. histolytica HM-1:IMSS. Our results, identifying expression profiles and patterns indicative of a virulence phenotype, may be useful in characterizing the transcriptional framework of virulence.

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