Roles of target cell membrane carbohydrate and lipid in Entamoeba histolytica interaction with mammalian cells

Bailey, Gordon B.; Gilmour, Jane; McCoomer, N E

doi:10.1128/iai.58.7.2389-2391.1990

Cited by 21 publications

(6 citation statements)

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“…Indeed, lectins such as the slime mold lectin discoidin I and the vertebrate elastin receptor may have different domains. The binding functions of some domains were insensitive to lectinspecific sugar residues (8), unlike the adherence and cytotoxicity of E. histolytica trophozoites (3,4,16,19,21,27,33). The binding domain on the amebic antigen did not correspond to the domain covered by the CD6 MAb or the 1553 and 1554 polyclonal antibodies.…”

Section: Discussionmentioning

confidence: 99%

“…To test interactions mediated by secretory products, enterocytic monolayers on tissue culture insert filters were explanted onto trophozoites cultured for 1 h on the bottom of the six-well dishes. To inhibit lectin-mediated interactions (3,33), experiments were done with the following sugars (Sigma, St. Louis, Mo. ): D-(ϩ)-galactose (100 mM); ␤-lactose (100 mM); N,NЈ,NЉ-triacetylchitotriose (40 mM); N-acetyl-D-galactosamine (100 mM); asialofetuin (1%); and heparin (200 IU/ml).…”

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confidence: 99%

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Contact-dependent transfer of the galactose-specific lectin of Entamoeba histolytica to the lateral surface of enterocytes in culture

et al. 1995

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In a study to investigate early interactions of Entamoeba histolytica with epithelial cell monolayers, we found that a monoclonal antibody (MAb), CD6, against an ameba surface antigen recognized the lateral surface of epithelial cells after coculture with trophozoites. Display of the CD6 antigen on the epithelial cells necessitated contact with active trophozoites. It was found neither at 4؇C, nor with prefixed trophozoites, nor with trophozoite-conditioned media, nor when a filter prevented direct contact. Monolayers exposed to amebic sonicates or detergent lysates showed random immunostaining. Access to the antigenic site was limited, as immunostaining occurred predominantly with subconfluent monolayers. CD6 epithelial cell binding was first observed after 5 min of coculture; trophozoite-mediated target cell lysis was not detected until 15 min following coculture. Epithelial cell immunostaining occurred with some other ameba-specific antibodies but not with MAbs raised against the 170-kDa subunit of the galactose-N-acetylgalactosamine (Gal/GalNAc)-specific lectin. The CD6 MAb as well as some other ameba-specific antibodies immunoprecipitated from trophozoite lysates the same bands as the MAbs against the cysteine-rich domain of the 170-kDa subunit of the Gal/GalNAcspecific lectin. Why the latter MAbs failed to stain epithelial cells in the vicinity of attached trophozoites is presently unknown. We concluded that E. histolytica trophozoites transferred the intact amebic Gal/GalNAcspecific lectin or a portion of it to the lateral surface of epithelial cells. This juxtacrine transfer preceded killing of target cells. MATERIALS AND METHODSTrophozoites. Trophozoites of E. histolytica HM1:IMSS (provided by H. Vermeersch, Laboratory of Pharmaceutical Technology, University of Ghent, Ghent, Belgium) were grown axenically at 35.5ЊC in 15-ml screw-cap tubes with TYI-S-33 medium (6), supplemented with 500 g of piperacillin per ml and 125 g of amikacin per ml. Trophozoites were harvested at the end of the logarithmic growth phase (72 h) by chilling at 4ЊC. They were concentrated at 200 ϫ g for 5 min and used immediately. For some experiments, freshly harvested trophozoites were fixed for 20 min in 3% paraformaldehyde (PF), washed in phosphatebuffered saline (PBS; pH 7.4) containing 0.9 mM Ca 2ϩ and 0.334 mM Mg 2ϩ (PBS Dϩ ), and quenched for 10 min with NH 4 Cl (50 mM in PBS E [Eisen formulation]). Thereafter, they were handled in the same way as live trophozoites. Conditioned medium was prepared from (i) logarithmic-growth-phase cultures in TYI-S-33; (ii) TYI-S-33, with or without serum, that had been incubated for 1 h with the total number of cells from an equal volume of a logarithmic-phase culture; and (iii) cocultures of trophozoites with mammalian cells as described below. Trophozoite cell extracts were prepared by one of the following methods: (i) intermittent sonication (Vibra Cell VC50; Sonics & Materials, Danbury, Conn.) of 2 ϫ 10 6 live trophozoites in 0.5 ml of PBS Dϩ on ice for a total of 45 s or (ii) vortexing...

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Contact-dependent transfer of the galactose-specific lectin of Entamoeba histolytica to the lateral surface of enterocytes in culture

et al. 1995

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“…Whereas, the carbohydrate recognition domain (CRD) is a region of lectins that binds to galactose (Gal) and Nacetylgalactosamine (GalNAc) and is confined to the heavy secondary unit (Hgl) [31]. Adhesion via Gal/GalNAc-lectin is a requirement for cell killing because in the absence of galactose or GalNAc, target cells are not killed by the E. histolytica.…”

Section: Virulence Factors 1 Adhesion Factormentioning

confidence: 99%

A review of entamoebahistolytica genome, virulence factors, phylogenetic tree and treatment

Alshaibani

2024

World Journal of Current Med and Pharm Research

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The study in this review aims to know and study the parasite Entamoebahistolytica that causes Amoebiasis worldwide. During its life cycle, E. histolytica passes through several phases, trophozoite stage, precyst stage, the cyst stage, the Metacyst stage, and Metacystictrophozoite stage. In this study, the spread of the parasite globally and in the Arab world and methods of treating the disease were also discussed. The Genomic structureof E. histolytica, like other organisms, is characterized by diversity and heterogeneity in its genetic content, which is one of the most important reasons for its survival and its ability to infect. Interestingly, the genome of the E. histolytica contains a large amount of genes presumed to be of bacterial origin. The study of the genetic diversity of E. histolytica gives paths to the developmental change that resulted in the emergence of evolutionary features or traits. Understanding amoebic virulence is important. Several studies have shown that genetic factors influence the virulence of parasitic infections. Studying the virulence of E. histolytica by Serine-rich protein (REHP) gene is among the important issues used in molecular epidemiological studies.

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“…Multiple lines of evidence suggest that actin also plays a major role in the process of particle uptake: actin ®laments are concentrated in the pseudopod and cytoplasm surrounding phagosomes (Wang et al, 1984), cytochalasin blocks phagocytosis by neutrophils and macrophages (Zigmond and Hirsch, 1972;Axline and Reaven, 1974) and F-actin assembles around IgG-coated erythrocytes during phagocytosis by macrophages (Greenberg et al, 1988). In the case of E. histolytica, rapid actin polymerization is observed upon contact with target cells (Bailey et al, 1985;Bailey et al, 1990;Voigt, 1999), which, in turn, can lead to an upregulation of the actin mRNA transcription level (Manning-Cela and Meza, 1997). Latex beads of similar size to erythrocytes are phagocytosed more slowly than red blood cells and do not induce an evident actin polymerization (Bailey et al, 1985), suggesting that speci®c ligand interactions play a role in inducing actin polymerization.…”

Section: Filamentous Actin Is Involved In Pseudopod Formationmentioning

confidence: 99%

New insights into the role of the cytoskeleton in phagocytosis of Entamoeba histolytica

Voigt

Guillén

1999

Cell Microbiol

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Entamoeba histolytica, a human parasite, crosses the natural barriers of the intestine and, in turn, spreads into the deeper organs, resulting in amoebiasis. The motility of the parasite and its ability to lyse or phagocytose human cells facilitates passage of the amoeba through the intestinal epithelium. Little is known about the uptake of material by this parasite; nevertheless, the cytoskeleton is believed to play a role in phagocytosis. Myosin IB, an actin‐binding protein, localizes to the phagocytic cup and, with time, surrounds the internalized phagosome itself. The role of unconventional myosins in phagocytosis has also been demonstrated in other cell types, suggesting that this molecular mechanism is a common denominator in phagocytic events. Here, we summarize the emerging view of the role of unconventional myosins as well as other cytoskeleton‐associated proteins in pseudopod formation at early stages of phagocytosis and during the late step of this process in E. histolytica.

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Roles of target cell membrane carbohydrate and lipid in Entamoeba histolytica interaction with mammalian cells

Cited by 21 publications

References 10 publications

Contact-dependent transfer of the galactose-specific lectin of Entamoeba histolytica to the lateral surface of enterocytes in culture

Contact-dependent transfer of the galactose-specific lectin of Entamoeba histolytica to the lateral surface of enterocytes in culture

A review of entamoebahistolytica genome, virulence factors, phylogenetic tree and treatment

New insights into the role of the cytoskeleton in phagocytosis of Entamoeba histolytica

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