Identification of a family of BspA like surface proteins of Entamoeba histolytica with novel leucine rich repeats

Davis, Paul H.; Zhang, Zhi; Chen, Minghe; Zhang, Xiaochun; Chakraborty, Subhra; Stanley, Samuel L.

doi:10.1016/j.molbiopara.2005.08.017

Cited by 42 publications

(40 citation statements)

References 18 publications

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“…One of E. histolytica BspA-like protein, EhLRRP1, has been shown to be localized on the cell surface, but its possible role in interaction with host ligands is not yet established [34]. As proposed in Trichomonas vaginalis , where BspA-like proteins might be involved in cell-cell adhesion when T.…”

Section: Resultsmentioning

confidence: 99%

Transcriptome Analysis of Encystation in Entamoeba invadens

et al. 2013

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Encystation is an essential differentiation process for the completion of the life cycle of a group of intestinal protozoa including Entamoeba histolytica, the causative agent of intestinal and extraintestinal amebiasis. However, regulation of gene expression during encystation is poorly understood. To comprehensively understand the process at the molecular level, the transcriptomic profiles of E . invadens , which is a related reptilian species that causes an invasive disease similar to that of E. histolytica, was investigated during encystation. Using a custom-generated Affymetrix platform microarray, we performed time course (0.5, 2, 8, 24, 48, and 120 h) gene expression analysis of encysting E . invadens . ANOVA analysis revealed that a total of 1,528 genes showed ≥3 fold up-regulation at one or more time points, relative to the trophozoite stage. Of these modulated genes, 8% (116 genes) were up-regulated at the early time points (0.5, 2 and 8h), while 63% (962 genes) were up-regulated at the later time points (24, 48, and 120 h). Twenty nine percent (450 genes) are either up-regulated at 2 to 5 time points or constitutively up-regulated in both early and late stages. Among the up-regulated genes are the genes encoding transporters, cytoskeletal proteins, proteins involved in vesicular trafficking (small GTPases), Myb transcription factors, cysteine proteases, components of the proteasome, and enzymes for chitin biosynthesis. This study represents the first kinetic analysis of gene expression during differentiation from the invasive trophozoite to the dormant, infective cyst stage in Entamoeba . Functional analysis on individual genes and their encoded products that are modulated during encystation may lead to the discovery of targets for the development of new chemotherapeutics that interfere with stage conversion of the parasite.

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Section: Resultsmentioning

confidence: 99%

Transcriptome Analysis of Encystation in Entamoeba invadens

et al. 2013

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“…Thus, we employed a more sensitive biochemical approach using the membrane-impermeant biotinylation reagent sulfo-NHS-LC-biotin to test if native calreticulin was present on the cell surface (16). The rationale was that calreticulin would be biotinylated only if it was exposed on the cell surface or secreted.…”

Section: Resultsmentioning

confidence: 99%

Entamoeba histolytica Cell Surface Calreticulin Binds Human C1q and Functions in Amebic Phagocytosis of Host Cells

et al. 2012

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ABSTRACTPhagocytosis of host cells is characteristic of tissue invasion by the intestinal amebaEntamoeba histolytica, which causes amebic dysentery and liver abscesses.Entamoeba histolyticainduces host cell apoptosis and uses ligands, including C1q, on apoptotic cells to engulf them. Two mass spectrometry analyses identified calreticulin in amebic phagosome preparations, and, in addition to its function as an endoplasmic reticulum chaperone, calreticulin is believed to be the macrophage receptor for C1q. The purpose of this study was to determine if calreticulin functions as anE. histolyticaC1q receptor during phagocytosis of host cells. Calreticulin was localized to the surface ofE. histolyticaduring interaction with both Jurkat lymphocytes and erythrocytes and was present in over 75% of phagocytic cups during amebic erythrophagocytosis. Presence of calreticulin on the cell surface was further demonstrated using a method that selectively biotinylated cell surface proteins and by flow cytometry using trophozoites overexpressing epitope-tagged calreticulin. Regulated overexpression of calreticulin increasedE. histolytica's ability to phagocytose apoptotic lymphocytes and calcium ionophore-treated erythrocytes but had no effect on amebic adherence to or destruction of cell monolayers or surface expression of the GalNAc lectin and serine-richE. histolyticaprotein (SREHP) receptors. Finally,E. histolyticacalreticulin bound specifically to apoptotic lymphocytes and to human C1q. Collectively, these data implicate cell surface calreticulin as a receptor for C1q duringE. histolyticaphagocytosis of host cells.

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“…1B. AdpC also showed significant similarity to a Bacteroides fragilis hypothetical protein (EMBL accession number BAD48495.1), a Bacteroides thetaiotaomicron hypothetical protein (GenBank accession number AA076347.1), the Streptococcus pneumoniae choline-binding protein PcpA (39), a Trichomonas vaginalis BspA-like surface antigen, and an Entamoeba histolytica BspA-like leucine-rich repeat protein (10,15,24).…”

Section: Characterization Of Adpc Using Bioinformatics Approachesmentioning

confidence: 99%

AdpC Is aPrevotella intermedia17 Leucine-Rich Repeat Internalin-Like Protein

et al. 2010

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The oral bacterium Prevotella intermedia attaches to and invades gingival epithelial cells, fibroblasts, and endothelial cells. Several genes encoding proteins that mediate both the adhesion and invasion processes are carried on the genome of this bacterium. Here, we characterized one such protein, AdpC, belonging to the leucine-rich repeat (LRR) protein family. Bioinformatics analysis revealed that this protein shares similarity with the Treponema pallidum LRR (LRR TP ) family of proteins and contains six LRRs. Despite the absence of a signal peptide, this protein is localized on the bacterial outer membrane, indicating that it is transported through an atypical secretion mechanism. The recombinant form of this protein (rAdpC) was shown to bind fibrinogen. In addition, the heterologous host strain Escherichia coli BL21 expressing rAdpC (V2846) invaded fibroblast NIH 3T3 cells at a 40-foldhigher frequency than control E. coli BL21 cells expressing a sham P. intermedia 17 protein. Although similar results were obtained by using human umbilical vein endothelial cells (HUVECs), only a 3-fold-increased invasion of V2846 into oral epithelial HN4 cells was observed. Thus, AdpC-mediated invasion is cell specific. This work demonstrated that AdpC is an important invasin protein of P. intermedia 17.

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Identification of a family of BspA like surface proteins of Entamoeba histolytica with novel leucine rich repeats

Cited by 42 publications

References 18 publications

Transcriptome Analysis of Encystation in Entamoeba invadens

Transcriptome Analysis of Encystation in Entamoeba invadens

Entamoeba histolytica Cell Surface Calreticulin Binds Human C1q and Functions in Amebic Phagocytosis of Host Cells

AdpC Is aPrevotella intermedia17 Leucine-Rich Repeat Internalin-Like Protein

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