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The Entamoeba histolytica Dnmt2 Homolog (Ehmeth) Confers Resistance to Nitrosative Stress

Hertz, Rivi ; Tovy, Ayala ; Kirschenbaum, Michael ; [et al.]

American Society for Microbiology ; 2014

In: Eukaryotic Cell Vol. 13, No. 4 ( 2014-04), p. 494-503

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In: Eukaryotic Cell, American Society for Microbiology, Vol. 13, No. 4 ( 2014-04), p. 494-503

Abstract: Nitric oxide (NO) has antimicrobial properties against many pathogens due to its reactivity as an S-nitrosylating agent. It inhibits many of the key enzymes that are involved in the metabolism and virulence of the parasite Entamoeba histolytica through S-nitrosylation of essential cysteine residues. Very little information is available on the mechanism of resistance to NO by pathogens in general and by this parasite in particular. Here, we report that exposure of the parasites to S -nitrosoglutathione (GSNO), an NO donor molecule, strongly reduces their viability and protein synthesis. However, the deleterious effects of NO were significantly reduced in trophozoites overexpressing Ehmeth, the cytosine-5 methyltransferase of the Dnmt2 family. Since these trophozoites also exhibited high levels of tRNA Asp methylation, the high levels suggested that Ehmeth-mediated tRNA Asp methylation is part of the resistance mechanism to NO. We previously reported that enolase, another glycolytic enzyme, binds to Ehmeth and inhibits its activity. We observed that the amount of Ehmeth-enolase complex was significantly reduced in GSNO-treated E. histolytica , which explains the aforementioned increase of tRNA methylation. Specifically, we demonstrated via site-directed mutagenesis that cysteine residues 228 and 229 of Ehmeth are susceptible to S-nitrosylation and are crucial for Ehmeth binding to enolase and for Ehmeth-mediated resistance to NO. These results indicate that Ehmeth has a central role in the response of the parasite to NO, and they contribute to the growing evidence that NO is a regulator of epigenetic mechanisms.

Type of Medium: Online Resource

ISSN: 1535-9778 , 1535-9786

URL: Article

DOI: 10.1128/EC.00031-14

Language: English

Publisher: American Society for Microbiology

Publication Date: 2014

detail.hit.zdb_id: 2071564-X

SSG: 12

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Down Regulation of Entamoeba histolytica Virulence by Monoxenic Cultivation with Escherichia coli O55 Is Related to a Decrease in Expression of the Light (35-Kilodalton) Subunit of the Gal/GalNAc Lectin

Padilla-Vaca, Felipe ; Sansonetti, P. J. ; Ankri, Serge ; [et al.]

American Society for Microbiology ; 1999

In: Infection and Immunity Vol. 67, No. 5 ( 1999-05), p. 2096-2102

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In: Infection and Immunity, American Society for Microbiology, Vol. 67, No. 5 ( 1999-05), p. 2096-2102

Abstract: Entamoeba histolytica virulence is related to a number of amebic components (lectins, cysteine proteinases, and amebapore) and host factors, such as intestinal bacterial flora. Trophozoites are selective in their interactions with bacteria, and the parasite recognition of glycoconjugates plays an important role in amebic virulence. Long-term monoxenic cultivation of pathogenic E. histolytica trophozoites, strains HK-9 or HM-1:IMSS, with Escherichia coli serotype O55, which binds strongly to the Gal/GalNAc amebic lectin, markedly reduced the trophozoites’ adherence and cytopathic activity on cell monolayers of baby hamster kidney (BHK) cells. Specific probes prepared from E. histolytica lectin genes as well as antibodies directed against the light (35-kDa) and heavy (170-kDa) subunits of the Gal/GalNAc lectin revealed a decrease in the transcription and expression of the light subunit in trophozoites grown monoxenically with E. coli O55. This effect was not observed when E. histolytica was grown with E. coli 346, a mannose-binding type I pilated bacteria. Our results suggest that the light subunit of the amebic lectin is involved in the modulation of parasite adherence and cytopathic activity.

Type of Medium: Online Resource

ISSN: 0019-9567 , 1098-5522

URL: Article

DOI: 10.1128/IAI.67.5.2096-2102.1999

RVK:

XA 10000

Language: English

Publisher: American Society for Microbiology

Publication Date: 1999

detail.hit.zdb_id: 1483247-1

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Molecular characterization of Entamoeba histolytica RNase III and AGO2, two RNA interference hallmark proteins

Abed, Mona ; Ankri, Serge

Elsevier BV ; 2005

In: Experimental Parasitology Vol. 110, No. 3 ( 2005-7), p. 265-269

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In: Experimental Parasitology, Elsevier BV, Vol. 110, No. 3 ( 2005-7), p. 265-269

Type of Medium: Online Resource

ISSN: 0014-4894

URL: Article

DOI: 10.1016/j.exppara.2005.02.023

Language: English

Publisher: Elsevier BV

Publication Date: 2005

detail.hit.zdb_id: 1466937-7

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Antimicrobial properties of allicin from garlic

Ankri, Serge ; Mirelman, David

Elsevier BV ; 1999

In: Microbes and Infection Vol. 1, No. 2 ( 1999-2), p. 125-129

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In: Microbes and Infection, Elsevier BV, Vol. 1, No. 2 ( 1999-2), p. 125-129

Type of Medium: Online Resource

ISSN: 1286-4579

URL: Article

DOI: 10.1016/S1286-4579(99)80003-3

Language: English

Publisher: Elsevier BV

Publication Date: 1999

detail.hit.zdb_id: 2019376-2

SSG: 12

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Pleiotropic phenotype in Entamoeba histolytica overexpressing DNA methyltransferase (Ehmeth)

Fisher, Ohad ; Siman-Tov, Rama ; Ankri, Serge

Elsevier BV ; 2006

In: Molecular and Biochemical Parasitology Vol. 147, No. 1 ( 2006-5), p. 48-54

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In: Molecular and Biochemical Parasitology, Elsevier BV, Vol. 147, No. 1 ( 2006-5), p. 48-54

Type of Medium: Online Resource

ISSN: 0166-6851

URL: Article

DOI: 10.1016/j.molbiopara.2006.01.007

Language: English

Publisher: Elsevier BV

Publication Date: 2006

detail.hit.zdb_id: 1491098-6

SSG: 12

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Enteric bacteria boost defences against oxidative stress in Entamoeba histolytica

Varet, Hugo ; Shaulov, Yana ; Sismeiro, Odile ; [et al.]

Springer Science and Business Media LLC ; 2018

In: Scientific Reports Vol. 8, No. 1 ( 2018-06-13)

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In: Scientific Reports, Springer Science and Business Media LLC, Vol. 8, No. 1 ( 2018-06-13)

Abstract: Oxidative stress is one of the strongest toxic factors in nature: it can harm or even kill cells. Cellular means of subverting the toxicity of oxidative stress are important for the success of infectious diseases. Many types of bacterium inhabit the intestine, where they can encounter pathogens. During oxidative stress, we analyzed the interplay between an intestinal parasite (the pathogenic amoeba Entamoeba histolytica - the agent of amoebiasis) and enteric bacteria (microbiome residents, pathogens and probiotics). We found that live enteric bacteria protected E. histolytica against oxidative stress. By high-throughput RNA sequencing, two amoebic regulatory modes were observed with enteric bacteria but not with probiotics. The first controls essential elements of homeostasis, and the second the levels of factors required for amoeba survival. Characteristic genes of both modes have been acquired by the amoebic genome through lateral transfer from the bacterial kingdom (e.g. glycolytic enzymes and leucine-rich proteins). Members of the leucine-rich are homologous to proteins from anti-bacterial innate immune such as Toll-like receptors. The factors identified here suggest that despite its old age in evolutionary terms, the protozoan E. histolytica displays key characteristics of higher eukaryotes’ innate immune systems indicating that components of innate immunity existed in the common ancestor of plants and animals.

Type of Medium: Online Resource

ISSN: 2045-2322

URL: Article

DOI: 10.1038/s41598-018-27086-w

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2018

detail.hit.zdb_id: 2615211-3

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Structural insights into Entamoeba histolytica arginase and structure‐based identification of novel non‐amino acid based inhibitors as potential antiamoebic molecules

Malik, Anjali ; Dalal, Vikram ; Ankri, Serge ; [et al.]

Wiley ; 2019

In: The FEBS Journal Vol. 286, No. 20 ( 2019-10), p. 4135-4155

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In: The FEBS Journal, Wiley, Vol. 286, No. 20 ( 2019-10), p. 4135-4155

Abstract: Arginase, the binuclear metalloenzyme, is a potential target for therapeutic intervention in protozoan infections. Entamoeba histolytica infection causes amebiasis which is the second most common cause of protozoan‐related human deaths after malaria. Here, we report the crystal structure of E. histolytica arginase ( Eh Arg) in complex with two known inhibitors N ω ‐hydroxy‐ l ‐arginine ( l ‐ NOHA ) and l ‐norvaline, and its product l ‐ornithine at 1.7, 2.0, and 2.4 Å, respectively. Structural and comparative analysis of Eh Arg–inhibitor complexes with human arginase revealed that despite only 33% sequence identity, the structural determinants of inhibitor recognition and binding are highly conserved in arginases with variation in oligomerization motifs. Knowledge regarding the spatial organization of residues making molecular contacts with inhibitory compounds enabled in the identification of four novel non‐amino acid inhibitors, namely irinotecan, argatroban, cortisone acetate, and sorafenib. In vitro testing of the in silico ‐identified inhibitors using purified enzyme proved that irinotecan, argatroban, cortisone acetate, and sorafenib inhibit Eh Arg with IC 50 value (m m ) of 1.99, 2.40, 0.91, and 2.75, respectively, as compared to the known inhibitors l ‐ NOHA and l ‐norvaline with IC 50 value (m m ) of 1.57 and 17.9, respectively. The identification of structure‐based non‐amino acid inhibitory molecules against arginase will be constructive in design and discovery of novel chemical modulators for treating amebiasis by directed therapeutics.

Type of Medium: Online Resource

ISSN: 1742-464X , 1742-4658

URL: Issue

URL: Article

DOI: 10.1111/febs.v286.20

DOI: 10.1111/febs.14960

Language: English

Publisher: Wiley

Publication Date: 2019

detail.hit.zdb_id: 2172518-4

SSG: 12

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Proteomic Identification of Oxidized Proteins in Entamoeba histolytica by Resin-Assisted Capture: Insights into the Role of Arginase in Resistance to Oxidative Stress

Shahi, Preeti ; Trebicz-Geffen, Meirav ; Nagaraja, Shruti ; [et al.]

Public Library of Science (PLoS) ; 2016

In: PLOS Neglected Tropical Diseases Vol. 10, No. 1 ( 2016-1-6), p. e0004340-

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In: PLOS Neglected Tropical Diseases, Public Library of Science (PLoS), Vol. 10, No. 1 ( 2016-1-6), p. e0004340-

Type of Medium: Online Resource

ISSN: 1935-2735

URL: Article

DOI: 10.1371/journal.pntd.0004340

DOI: 10.1371/journal.pntd.0004340.g001

DOI: 10.1371/journal.pntd.0004340.g002

DOI: 10.1371/journal.pntd.0004340.g003

DOI: 10.1371/journal.pntd.0004340.g004

DOI: 10.1371/journal.pntd.0004340.g005

DOI: 10.1371/journal.pntd.0004340.t001

DOI: 10.1371/journal.pntd.0004340.t002

DOI: 10.1371/journal.pntd.0004340.t003

DOI: 10.1371/journal.pntd.0004340.s001

DOI: 10.1371/journal.pntd.0004340.s002

DOI: 10.1371/journal.pntd.0004340.s003

DOI: 10.1371/journal.pntd.0004340.s004

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2016

detail.hit.zdb_id: 2429704-5

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Escherichia coli mediated resistance of Entamoeba histolytica to oxidative stress is triggered by oxaloacetate

Shaulov, Yana ; Shimokawa, Chikako ; Trebicz-Geffen, Meirav ; [et al.]

Public Library of Science (PLoS) ; 2018

In: PLOS Pathogens Vol. 14, No. 10 ( 2018-10-11), p. e1007295-

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In: PLOS Pathogens, Public Library of Science (PLoS), Vol. 14, No. 10 ( 2018-10-11), p. e1007295-

Type of Medium: Online Resource

ISSN: 1553-7374

URL: Article

DOI: 10.1371/journal.ppat.1007295

DOI: 10.1371/journal.ppat.1007295.g001

DOI: 10.1371/journal.ppat.1007295.g002

DOI: 10.1371/journal.ppat.1007295.g003

DOI: 10.1371/journal.ppat.1007295.g004

DOI: 10.1371/journal.ppat.1007295.g005

DOI: 10.1371/journal.ppat.1007295.g006

DOI: 10.1371/journal.ppat.1007295.g007

DOI: 10.1371/journal.ppat.1007295.g008

DOI: 10.1371/journal.ppat.1007295.g009

DOI: 10.1371/journal.ppat.1007295.t001

DOI: 10.1371/journal.ppat.1007295.t002

DOI: 10.1371/journal.ppat.1007295.s001

DOI: 10.1371/journal.ppat.1007295.s002

DOI: 10.1371/journal.ppat.1007295.s003

DOI: 10.1371/journal.ppat.1007295.s004

DOI: 10.1371/journal.ppat.1007295.s005

DOI: 10.1371/journal.ppat.1007295.s006

DOI: 10.1371/journal.ppat.1007295.s007

DOI: 10.1371/journal.ppat.1007295.s008

DOI: 10.1371/journal.ppat.1007295.s009

DOI: 10.1371/journal.ppat.1007295.s010

DOI: 10.1371/journal.ppat.1007295.s011

DOI: 10.1371/journal.ppat.1007295.s012

DOI: 10.1371/journal.ppat.1007295.s013

DOI: 10.1371/journal.ppat.1007295.s014

DOI: 10.1371/journal.ppat.1007295.s015

DOI: 10.1371/journal.ppat.1007295.s016

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2018

detail.hit.zdb_id: 2205412-1

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A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Activity

Tovy, Ayala ; Siman Tov, Rama ; Gaentzsch, Ricarda ; [et al.]

Public Library of Science (PLoS) ; 2010

In: PLoS Pathogens Vol. 6, No. 2 ( 2010-2-19), p. e1000775-

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In: PLoS Pathogens, Public Library of Science (PLoS), Vol. 6, No. 2 ( 2010-2-19), p. e1000775-

Type of Medium: Online Resource

ISSN: 1553-7374

URL: Article

DOI: 10.1371/journal.ppat.1000775

DOI: 10.1371/journal.ppat.1000775.g001

DOI: 10.1371/journal.ppat.1000775.g002

DOI: 10.1371/journal.ppat.1000775.g003

DOI: 10.1371/journal.ppat.1000775.g004

DOI: 10.1371/journal.ppat.1000775.g005

DOI: 10.1371/journal.ppat.1000775.g006

DOI: 10.1371/journal.ppat.1000775.g007

DOI: 10.1371/journal.ppat.1000775.t001

DOI: 10.1371/journal.ppat.1000775.s001

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2010

detail.hit.zdb_id: 2205412-1

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