Amebiasis.

Bruckner, David A.

doi:10.1128/cmr.5.4.356-369.1992

Cited by 2 publications

(2 citation statements)

References 100 publications

(153 reference statements)

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“…The trophozoites in the colon also undergo encystation to convert into cysts and are excreted out of the host body to continue the life cycle. The interconversion between the trophozoites and the cysts is the key factor in the survival of the pathogen and its transmission from one host to another (Bruckner, 1992).…”

Section: Introductionmentioning

confidence: 99%

EhRho6‐mediated actin degradation in Entamoeba histolytica is associated with compromised pathogenicity

Narooka

Apte

Yadav

et al. 2022

Molecular Microbiology

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Entamoeba histolytica causes amoebiasis which is a major health concern in developing countries. E. histolytica pathogenicity has been implicated to a large repertoire of small GTPases which switch between the inactive GDP bound state and the active GTP bound state with the help of guanine nucleotide exchange factors (GEFs) and GTPase activating protein (GAPs). Rho family of small GTPases are well known to modulate the actin cytoskeletal dynamics which plays a major role in E. histolytica pathogenicity. Here, we report an atypical amoebic RhoGEF, and its preferred substrate EhRho6, which, upon overexpression abrogated the pathogenic behavior of the amoeba such as adhesion to host cell, monolayer destruction, erythrophagocytosis, and formation of actin dots. A causative immunoblot analysis revealed actin degradation in the EhRho6 overexpressing trophozoites that could be inhibited by blocking the amoebic proteasomal pathway. A careful analysis of the results from a previously published transcriptomics study, in conjunction with our observations, led to the identification of a clade of Rho GTPases in this pathogenic amoeba which we hypothesize to have implications during the amoebic encystation.

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Section: Introductionmentioning

confidence: 99%

EhRho6‐mediated actin degradation in Entamoeba histolytica is associated with compromised pathogenicity

Narooka

Apte

Yadav

et al. 2022

Molecular Microbiology

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“…Entamoeba histolytica is the etiological agent of amebiasis. It is estimated that this protozoan parasite infects 500 million people worldwide (its prevalence is around 1% in industrialized countries and reaches 50–80% in tropical countries, causing 40,000–110,000 deaths per year) [ 1 - 3 ]. Phagocytosis of epithelial cells, erythrocytes, leucocytes and bacteria from the commensal microbiota is a major pathogenic mechanism used by E. histolytica .…”

Section: Introductionmentioning

confidence: 99%

A Toll/IL-1R/resistance domain-containing thioredoxin regulates phagocytosis in Entamoeba histolytica

et al. 2012

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BackgroundEntamoeba histolytica is a protozoan parasite that infects humans and causes amebiasis affecting developing countries. Phagocytosis of epithelial cells, erythrocytes, leucocytes, and commensal microbiota bacteria is a major pathogenic mechanism used by this parasite. A Toll/IL-1R/Resistance (TIR) domain-containing protein is required in phagocytosis in the social ameba Dictyostelium discoideum, an ameba closely related to Entamoeba histolytica in phylogeny. In insects and vertebrates, TIR domain-containing proteins regulate phagocytic and cell activation. Therefore, we investigated whether E. histolytica expresses TIR domain-containing molecules that may be involved in the phagocytosis of erythrocytes and bacteria.MethodsUsing in silico analysis we explored in Entamoeba histolytica databases for TIR domain containing sequences. After silencing TIR domain containing sequences in trophozoites by siRNA we evaluated phagocytosis of erythrocytes and bacteria.ResultsWe identified an E. histolytica thioredoxin containing a TIR-like domain. The secondary and tertiary structure of this sequence exhibited structural similarity to TIR domain family. Thioredoxin transcripts silenced in E. histolytica trophozoites decreased erythrocytes and E. coli phagocytosis.ConclusionTIR domain-containing thioredoxin of E. histolytica could be an important element in erythrocytes and bacteria phagocytosis.

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Amebiasis.

Cited by 2 publications

References 100 publications

EhRho6‐mediated actin degradation in Entamoeba histolytica is associated with compromised pathogenicity

EhRho6‐mediated actin degradation in Entamoeba histolytica is associated with compromised pathogenicity

A Toll/IL-1R/resistance domain-containing thioredoxin regulates phagocytosis in Entamoeba histolytica

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