Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Secretome study for human hepatic model during entamoeba invasion

ABSTRACT: Investigations of human parasitic diseases depend on the availability of appropriate in vivo animal models and ex vivo experimental systems, and are particularly difficult for pathogens whose exclusive natural hosts are humans, as for Entamoeba histolytica, the protozoan parasite responsible for amoebiasis. We elaborated a human hepatic in vitro model consisting of cultured liver sinusoidal endothelial cells and hepatocytes in a 3D collagen-I environment. We have characterized the model's barrier function, its chemical and structural complexity and examined E. histolytica invasion. This study deals with secretome of hepatic model under various invasion conditions.

INSTRUMENT(S):

ORGANISM(S): Bos Taurus (bovine) Homo Sapiens (human) Entamoeba Histolytica Hm-1:imss-a

SUBMITTER: gagan jhingan

LAB HEAD: Nancy Guillen

PROVIDER: PXD000893 | Pride | 2014-08-13

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	2013-08-02_GAG_Top10_GJ200_collagen1A.raw	Raw
	2013-08-02_GAG_Top10_GJ200_collagen1A_Search_EntamoebaDB.msf	Msf
	2013-08-02_GAG_Top10_GJ200_collagen1A_Search_EntamoebaDB.pep.xml	Pepxml
	2013-08-02_GAG_Top10_GJ200_collagen1A_Search_bovineDB.msf	Msf
	2013-08-02_GAG_Top10_GJ200_collagen1A_Search_bovineDB.pep.xml	Pepxml

Items per page:

1 - 5 of 105

Similar Datasets

Autophosphorylation of Entamoeba histolytica atypical kinase EhAK1

Project description:Phagocytosis plays a key role in survival and pathogenicity of Entamoeba histolytica. We have recently demonstrated that an atypical kinase EhAK1 is involved in phagocytosis in this parasite. It is recruited to the phagocytic cups through interaction with EhCaBP1. EhAK1 manipulates actin dynamics by multiple mechanisms including phosphorylation of G-actin. Biochemical analysis showed that EhAK1 is a serine/threonine kinase with broad ion specificity and undergoes multiple trans-autophosphorylation. Multiple autophosphorylation sites were identified by mass spectrometry. Out of these Thr279 appears to be involved in both autophosphorylation as well as substrate phosphorylation.

2018-10-24 | PXD002691 | Pride

Whole genome bisulfite sequencing of Entamoeba histolytica

Project description:Up until now, the existence of Dnmt2-mediated DNA methylation has mostly been supported by focal analyses in organisms that contain Dnmt2, but no Dnmt1 or Dnmt3 DNA methyltransferase. In these organisms, several independent studies have also provided support for a biologically important function of Dnmt2-dependent DNA methylation. For example, Dnmt2-dependent methylation in Entamoeba histolytica, the causative agent of amebic dysentery, has been connected to the parasite s virulence. However, global DNA methylation levels in Entamoeba have been found to be very low. In addition, no specific features, such as CpG-specificity and specificity for certain genetic subcompartments have been described. This distinguishes Dnmt2-dependent methylation patterns from all other known methylomes and has raised questions about the validity of the underlying results. We have used whole-genome bisulfite sequencing for an unbiased characterization of the Entamoeba histolytica methylome at single-base resolution in a E.histolytica strain HM-1:IMSS devoid of significant level of EhDnmt2 (Ehmeth) expression. Paired-end BS-sequencing was performed on an Illumina Genome Analyzer with read lengths of 105 base pairs and an average insert size of 200 bp.

2011-08-10 | E-GEOD-31295 | biostudies-arrayexpress

Small RNAs during E. histolytica stress response

Project description:We analyzed ~27nt small RNAs from Entamoeba histolytica trophozoites in basal conditions and after heat shock or oxidative stress E. histolytica trophozoites were treated with 1mM H2O2 for 1hr, or heat shocked at 42°C for 1hr and RNA was isolated and small RNA populations were compared to small RNA populations from untreated trophozoites

2015-07-22 | E-GEOD-67230 | biostudies-arrayexpress

Transcriptional profiling of human liver sinusoidal endothelial cells respond to interaction with Entamoeba histolityca.

Project description:incubation for 15 min and 30 min of human liver sinusoidal cell cultures with virulent or virulence-attenuated Entamoeba histolytica or incubation without parasites added

2011-01-01 | E-MEXP-2572 | biostudies-arrayexpress

Phagosome proteome of mock and Atg8 silenced Entamoeba histolytica strains

Project description:The enteric protozoan parasite Entamoeba histolytica have high phagocytic ability. Phagocytosis is also important for the pathogenicity of this parasite; molecular mechanisms of phagocytosis and phagosome maturation is focused. Atg8 is well studied autophagy marker protein. We previously shown that E. histolytica Atg8 translocate to nascent trogosomes and expression silencing of the Atg8 caused retardation of phagosome acidification. To investigate how Atg8 regulates phagosome maturation, here we conducted proteome analysis of phagosomes isolated from an E. histolytica strain in which atg8 gene expression are silenced (atg8 gene silenced, atg8-gs) and its mock control strain (transfected with psAP2-Gunma).

2022-10-20 | PXD034376 | Pride

Entamoeba histolytica nuclear proteome

Project description:The polyadenylation factor EhCFIm25 has been recently reported as a biochemical target in Entamoeba histolytica. The prediction and experimental characterization of its interactome revealed close relationships between proteins involved in gene expression regulation and enzymes of energy metabolism. Here, the identification of the nuclear proteome of E. histolytica by mass spectrometry analysis showed the presence of typically cytoplasmic proteins in the nuclear compartment, which could have moonlight functions. Prediction of PPI network confirmed the relevance of some metabolic enzymes in the coordination between energy and RNA metabolism, opening new perspectives for human amoebiasis control.

2025-06-09 | PXD056950 | Pride

comparative phosphoproteomics uncover proteins from the mechanobiome in Entamoeba histolytica

Project description:Entamoeba histolytica is a protozoan parasite and the causative agent of amoebiasis in humans. This amoeba invades human tissues by taking advantage of the actin-rich cytoskeleton to move, enter the tissue matrix, kill and phagocyte human cells. During events leading to tissue invasion, E. histolytica moves from the intestinal lumen to cross the mucus layer and enter the epithelial parenchyma. Faced with the chemical and physical constraints of these diverse environments, E. histolytica has developed sophisticated systems to integrate internal and external signals and to coordinate cell shape changes and motility. These cell signalling circuits are driven by the interactions between the parasite and the extracellular matrix combined with rapid responses from the mechanobiome protein network in which protein phosphorylation is important. To understand phosphorylation events we focus on phosphatidylinositol 3-kinases and we have performed live cell imaging and phosphoproteomics. The results highlight 1150 proteins within the amoebic proteome being members of the phosphoproteome, including signalling and structural molecules involved in cytoskeleton activities. Inhibition of phosphatidylinositol 3-kinases alters phosphorylation dynamics in important members of these categories, a finding that correlates with changes in the kinetic parameters of amoeba motility and morphology, as well as with altered content of actin-rich adhesive structures

2023-05-15 | PXD040787 | Pride

Small RNA pyrosequencing in the protozoan parasite Entamoeba histolytica reveals strain-specific small RNAs that target virulence genes

Project description:We provided a full spectrum analysis for E. histolytica AGO2-2 associated 27nt small RNAs. Additionally, comparative analysis of small RNA populations from virulent and non-virulent amebic strains indicates that small RNA populations may regulate virulence genes. AGO2-2 bound small RNAs from E. histolytica strain HM-1:IMSS were immunoprecipitated and sequenced using 454 technology. Three independant sequencing runs were perfomed using the same RNA sample. In addition, size selected small RNAs from E. histolytica strain Rahman were sequenced with the same technology. One sequencing run was performed on this sample.

2013-01-24 | E-GEOD-43668 | biostudies-arrayexpress

Coactosin phosphorylation controls Entamoeba histolytica 1 cell membrane protusions and cell motility

Project description:Invasion of the colon wall by Entamoeba histolytica during amoebic dysentery entails migration of trophozoites through tissue layers that are rich in extracellular matrix (ECM). Transcriptional silencing of the E. histolytica matrix surface metalloprotease EhMSP-1 produces hyper-adherent, less motile trophozoites that are deficient in forming invadosomes. Reversible protein phosphorylation is often implicated in regulation of cell motility and invadosome formation. To identify such intermediaries of the EhMSP-1 silenced phenotype, here we compared the phosphoproteome of EhMSP-1 silenced and vector control trophozoites using quantitative mass spectrometry based proteomics. Six proteins were found to be differentially phosphorylated in EhMSP-1 silenced and control cells, including EhCoactosin, a member of the ADF/Cofilin family of actin binding proteins, which was hyperphosphorylated at serine 147 (S147). Regulated over-expression of wild type, phosphomimetic (S147D), and non phosphorylatable (S147A) EhCoactosin variants was used to test if S147 phosphorylation functions in control of E. histolytica actin dynamics. Each of the over-expressed proteins co37 localized with F-actin during E. histolytica phagocytosis. Nonetheless, trophozoites overexpressing EhCoactosin S147D formed more and poorly coordinated small membrane protrusions compared to control or S147A expressing cells, while trophozoites overexpressing EhCoactosin S147A were significantly more motile within a model of mammalian ECM. Therefore, although EhCoactosin’s actin-binding ability appeared unaffected by S147 phosphorylation, EhCoactosin phosphorylation helps to regulate amoebic motility. These data help to understand the mechanisms underlying altered adherence and motility in EhMSP-1 silenced trophozoites, and lay the groundwork for identifying kinases and phosphatases critical for control of amoebic invasiveness.

2020-07-15 | PXD018276 | Pride

Gene expression in phagocytic and non-phagocytic Entamoeba histolytica populations

Project description:The ability of Entamoeba histolytica to phagocytose host cells correlates to observed virulence in vivo. To better understand the mechanism of phagocytosis we used paramagnetic beads coated with host ligand and sorted trophozoites based on phagocytic ability. Gene expression was then measured in both the sorted phagocytic and non-phagocytic populations using a custom Affymetrix chip for E. histolytica. Feed forward regulation of phagocytosis by Entamoeba histolytica. Infection and Immunity. PMID 23045476

2012-10-16 | GSE41604 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data