• Title/Summary/Keyword: (co)amoeba

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The effect of silica on the development of experimental Acanthamoeba meningoencephalitis with reference to the macrophage role in mice (Acmthmoeba culbertsoni 감염에 대한 silica 투여의 영향 - 대식세포의 역할을 중심으로 -)

  • 이홍수;신호준
    • Parasites, Hosts and Diseases
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    • v.32 no.4
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    • pp.259-266
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    • 1994
  • The role of macrophages was observed In intranasally infected CSH/HeJ mice with trophozoites (3 ×105) of Acnnthomoeba culbertsoni which was a kind of free-living amoebae inducing meningoencephalitis in human and experimental animals. The mortality was 60% in the group of intraperitoneally injected mice with silica (0.5 mg/0.5 ml). It was much higher than that of 10% in the group of amoeba infected mice without silica administration. The phagocytic index of peritoneal macrophages co-cultured with Toxoplasma gondii was estimated daily. In contrast to the control and amoeba infected group which didn't show significant fluctuation of the phagocytic indices, the silica administrated group revealed under 3% until day 3, and gradual increase up to 24.7% in day 5 which was same level of amoeba infected group without silica administration. The level of interleukin- lb (IL- lb) measured by ELISA was the highest in the amoeba infected group without silica injection and the lowest in the amoeba infected group with silica administration. In the test of the amoebicidal activity of mice peritoneal macrcphages Dl uitro, silica administration revealed reducing effect on amoebicidal activity of macrophages. In conclusion, macrophages were proven to play a significant role in defense mechanism against the development of experimentally induced Acnnthamoebo menigoencephalitis.

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Cytopathic Change and Inflammatory Response of Human Corneal Epithelial Cells Induced by Acanthamoeba castellanii Trophozoites and Cysts

  • Sohn, Hae-Jin;Seo, Ga-Eun;Lee, Jae-Ho;Ham, A-Jeong;Oh, Young-Hwan;Kang, Heekyoung;Shin, Ho-Joon
    • Parasites, Hosts and Diseases
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    • v.57 no.3
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    • pp.217-223
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    • 2019
  • Acanthamoeba castellanii has ubiquitous distribution and causes primary acanthamoebic keratitis (AK). AK is a common disease in contact lens wearers and results in permanent visual impairment or blindness. In this study, we observed the cytopathic effect, in vitro cytotoxicity, and secretion pattern of cytokines in human corneal epithelial cells (HCECs) induced by A. castellanii trophozoites and/or cysts. Morphological observation revealed that panked dendritic HCECs co-cultured with amoeba cysts had changed into round shape and gradually died. Such changes were more severe in co-culture with cyst than those of co-cultivation with trophozoites. In vitro cytotoxicity assay revealed the highest cytotoxicity to HCECs in the co-culture system with amoeba cysts. A. castellanii induced the expression of $IL-1{\alpha}$, IL-6, IL-8, and CXCL1 in HCECs. Secreted levels of $IL-1{\alpha}$, IL-6, and IL-8 in HCECs co-cultured with both trophozoites and cysts were increased at an early incubation time (3 and 6 hr). These results suggested that cytopathic changes and pro-inflammatory cytokines release of HCECs in response to A. castellanii, especially amoebic cysts, are an important mechanism for AK development.

A NATURAL TOPOLOGICAL MANIFOLD STRUCTURE OF PHASE TROPICAL HYPERSURFACES

  • Kim, Young Rock;Nisse, Mounir
    • Journal of the Korean Mathematical Society
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    • v.58 no.2
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    • pp.451-471
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    • 2021
  • First, we define phase tropical hypersurfaces in terms of a degeneration data of smooth complex algebraic hypersurfaces in (ℂ∗)n. Next, we prove that complex hyperplanes are homeomorphic to their degeneration called phase tropical hyperplanes. More generally, using Mikhalkin's decomposition into pairs-of-pants of smooth algebraic hypersurfaces, we show that a phase tropical hypersurface with smooth tropicalization is naturally a topological manifold. Moreover, we prove that a phase tropical hypersurface is naturally homeomorphic to a symplectic manifold.

Cytotoxicity of target cell against Naegleria fowleri under non-contact condition (비접촉 조건에서의 Naegleria fowleri에 의한 표적세포의 세포독성)

  • Kang, Changgeun;Hong, Il-Hwa;Kim, Jong-Hyun
    • Korean Journal of Veterinary Service
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    • v.42 no.4
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    • pp.169-175
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    • 2019
  • Naegleria fowleri, a pathogenic free-living amoeba, leads to a fatal infection known as primary amebic meningoencephalitis (PAM) in human and animals. PAM is an acute, fulminant, necrotizing, and hemorrhagic disease that leads to death in approximately seven days. In this study, we investigate the cytotoxicity of target cells and the secreted molecules of N. fowleri under the non-contact condition. The target cell (U87MG cell) treated with N. fowleri lysates showed no morphological changes and no cytotoxicity. By contrast, the U87MG cells co-cultured with N. fowleri trophozoites under the non-contact condition induced morphological changes and reduction in number. When U87MG cells were co-cultured with N. fowleri trophozoites under the non-contact condition for 30 min, 2 hr, and 4 hr, the levels of cytotoxicity of target cells were 32.3, 35.5, and 37.8%, respectively. Particularly, when the ratio of amoeba to target cells is 10 to 1, the level of cytotoxicity of target cells was 49.7% at 30 min. To show the proteins secreted from N. fowleri under the non-contact condition, we carried out 2D electrophoresis and observed 6 major proteins. Finally, these results suggest that the molecules released from N. fowleri under the non-contact condition induce the cell death and this process is an important step in pathogenesis of N. fowleri.

Naegleria fowleri Induces Jurkat T Cell Death via O-deGlcNAcylation

  • Lee, Young Ah;Kim, Kyeong Ah;Shin, Myeong Heon
    • Parasites, Hosts and Diseases
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    • v.59 no.5
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    • pp.501-505
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    • 2021
  • The pathogenic free-living amoeba Naegleria fowleri causes primary amoebic meningoencephalitis, a fatal infection, by penetrating the nasal mucosa and migrating to the brain via the olfactory nerves. N. fowleri can induce host cell death via lytic necrosis. Similar to phosphorylation, O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation (O-GlcNAcylation) is involved in various cell-signaling processes, including apoptosis and proliferation, with O-GlcNAc addition and removal regulated by O-GlcNAc transferase and O-GlcNAcase (OGA), respectively. However, the detailed mechanism of host cell death induced by N. fowleri is unknown. In this study, we investigated whether N. fowleri can induce the modulation of O-GlcNAcylated proteins during cell death in Jurkat T cells. Co-incubation with live N. fowleri trophozoites increased DNA fragmentation. In addition, incubation with N. fowleri induced a dramatic reduction in O-GlcNAcylated protein levels in 30 min. Moreover, pretreatment of Jurkat T cells with the OGA inhibitor PUGNAc prevented N. fowleri-induced O-deGlcNAcylation and DNA fragmentation. These results suggest that O-deGlcNAcylation is an important signaling process that occurs during Jurkat T cell death induced by N. fowleri.

Involvement of NOX2-derived ROS in human hepatoma HepG2 cell death induced by Entamoeba histolytica

  • Young Ah Lee ;Myeong Heon Shin
    • Parasites, Hosts and Diseases
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    • v.61 no.4
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    • pp.388-396
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    • 2023
  • Entamoeba histolytica is an enteric tissue-invasive protozoan parasite causing amoebic colitis and liver abscesses in humans. Amoebic contact with host cells activates intracellular signaling pathways that lead to host cell death via generation of caspase-3, calpain, Ca2+ elevation, and reactive oxygen species (ROS). We previously reported that various NADPH oxidases (NOXs) are responsible for ROS-dependent death of various host cells induced by amoeba. In the present study, we investigated the specific NOX isoform involved in ROS-dependent death of hepatocytes induced by amoebas. Co-incubation of hepatoma HepG2 cells with live amoebic trophozoites resulted in remarkably increased DNA fragmentation compared to cells incubated with medium alone. HepG2 cells that adhered to amoebic trophozoites showed strong dichlorodihydrofluorescein diacetate (DCF-DA) fluorescence, suggesting intracellular ROS accumulation within host cells stimulated by amoebic trophozoites. Pretreatment of HepG2 cells with the general NOX inhibitor DPI or NOX2-specific inhibitor GSK 2795039 reduced Entamoeba-induced ROS generation. Similarly, Entamoeba-induced LDH release from HepG2 cells was effectively inhibited by pretreatment with DPI or GSK 2795039. In NOX2-silenced HepG2 cells, Entamoeba-induced LDH release was also significantly inhibited compared with controls. Taken together, the results support an important role of NOX2-derived ROS in hepatocyte death induced by E. histolytica.

Molecular and biochemical characterization of a novel actin bundling protein in Acanthamoeba

  • Alafag Joanna It-itan;Moon Eun-Kyung;Hong Yeon-Chul;Chung Dong-Il;Kong Hyun-Hee
    • Parasites, Hosts and Diseases
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    • v.44 no.4 s.140
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    • pp.331-341
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    • 2006
  • Actin binding proteins play key roles in cell structure and movement particularly as regulators of the assembly, stability and localization of actin filaments in the cytoplasm. In the present study, a cDNA clone encoding an actin bundling protein named as AhABP was isolated from Acanthamoeba healyi, a causative agent of granulomatous amebic encephalitis. This clone exhibited high similarity with genes of Physarum polycephalum and Dictyostelium discoideum, which encode actin bundling proteins. Domain search analysis revealed the presence of essential conserved regions, i.e., an active actin binding site and 2 putative calcium binding EF-hands. Transfected amoeba cells demonstrated that AhABP is primarily localized in phagocytic cups, peripheral edges, pseudopods, and in cortical cytoplasm where actins are most abundant. Moreover, AhABP after the deletion of essential regions formed ellipsoidal inclusions within transfected cells. High-speed co-sedimentation assays revealed that AhABP directly interacted with actin in the presence of up to $10{\mu}M$ of calcium. Under the electron microscope, thick parallel bundles were formed by full length AhABP, in contrast to the thin actin bundles formed by constructs with deletion sites. In the light of these results, we conclude that AhABP is a novel actin bundling protein that is importantly associated with actin filaments in the cytoplasm.