Antisense Inhibition of Expression of Cysteine Proteinases Affects
            <i>Entamoeba histolytica</i>
            -Induced Formation of Liver Abscess in Hamsters

Ankri, Serge; Stolarsky, Tamara; Bracha, Rivka; Padilla‐Vaca, Felipe; Mirelman, David

doi:10.1128/iai.67.1.421-422.1999

Cited by 128 publications

(50 citation statements)

References 18 publications

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“…In EHI_127670-silencing transfectants, a lower activity for EhCP-A1 and EhCP-A5 can be detected. This result supports the major role for these peptidases (especially EhCP-A5) in tissue destruction, as previously shown (25,26,34,35). However, it has not been possible to clarify which mechanism underlies the inhibition identified hererin.…”

Section: Discussionsupporting

confidence: 89%

Trigger‐induced RNAi gene silencing to identify pathogenicity factors of Entamoeba histolytica

et al. 2018

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Recently, Entamoeba histolytica clones derived from isolate HM-1:IMSS that differ in their pathogenicity were identified. Whereas some clones induce amoebic liver abscesses (ALAs) in animal models of amoebiasis, others provoke only minimal liver lesions. Based on transcriptome studies of pathogenic and nonpathogenic clones, differentially expressed genes associated with reduced or increased liver pathology can be identified. Here, to analyze the influence of these genes on ALA formation in more detail, an RNA interference-trigger mediated silencing approach was used. Using newly identified trigger sequences, the expression of 15 genes was silenced. The respective transfectants were analyzed for their ability to induce liver destruction in the murine model for the disease. Silencing of EHI_180390 (encoding an AIG1 protein) increased liver pathology induced by a nonpathogenic parent clone, whereas silencing of EHI_127670 (encoding a hypothetical protein) decreased the pathogenicity of an initially pathogenic parent clone. Additional phenotypical in vitro analyses of EHI_127670 silencing as well as overexpression transfectants indicated that this molecule has an influence on size, growth, and cysteine peptidase activity of E. histolytica. This work describes an example of how the sole operational method for effective gene silencing in E. histolytica can be used for comprehensive analyses of putative pathogenicity factors.-Matthiesen, J., Lender, C., Haferkorn, A., Fehling, H., Meyer, M., Matthies, T., Tannich, E., Roeder, T., Lotter, H., Bruchhaus, I. Trigger-induced RNAi gene silencing to identify pathogenicity factors of Entamoeba histolytica.

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Section: Discussionsupporting

confidence: 89%

Trigger‐induced RNAi gene silencing to identify pathogenicity factors of Entamoeba histolytica

et al. 2018

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“…The role of several CPs in the virulence of protozoan parasites, such as Trichomonas vaginalis (Alvarez-Sanchez et al, 2000), Leishmania major (Joshi et al, 2002), Trypanosoma cruzi (Tomas et al, 1997), Plasmodium vivax (Rosenthal et al, 1994) or E. histolytica (Ankri et al, 1999) has been conclusively demonstrated. Additionally, the functional versatility of CPs and the relevant role that they play in virulence make these molecules promising chemotherapeutic or vaccine targets (McKerrow, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…In general, CPs participate in invasion of tissues by E. histolytica trophozoites (Reed et al, 1989b;Bruchhaus et al, 1996;Ankri et al, 1999). During invasion, CPs face different substrates in the host, mainly those forming the extracellular matrix, which may be degraded to allow the trophozoite invasion.…”

Section: Rehcp112 Degrades Collagen Type I Fibronectin and Destroys mentioning

confidence: 99%

EhCP112 is an Entamoeba histolytica secreted cysteine protease that may be involved in the parasite-virulence

Ocadiz¹,

Orozco²,

Carrillo³

et al. 2004

Cellular Microbiology

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SummaryEhCP112 is an Entamoeba histolytica protease that together with the EhADH112 protein forms the EhC-PADH complex involved in trophozoite virulence. Here, we produced the recombinant EhCP112 and studied its relationships with extracellular matrix components and with target cells. A DNA fragment containing the pro-peptide and the mature enzyme was expressed in bacteria as an active enzyme (rEhCP112), whereas the full gene containing the signal peptide, the pro-peptide and the mature enzyme expressed a non-active protein. The fragment only with the mature enzyme was not expressed. rEhCP112 purified by affinity columns digested azocasein and had a strong autoproteolytic activity. Four hours after purification the protein appeared degraded. Anti-tag antibodies, monoclonal antibodies against the EhCP112 and sera from human patients with amoebiasis recognized rEhCP112. rEhCP112 digested gelatin, collagen type I, fibronectin and haemoglobin; it destroyed MDCK cell monolayers and bound to red blood cells. The native EhCP112 was poorly expressed in a virulence-deficient mutant, and in the wild-type clone it was located in secreted vesicles, forming the EhCPADH complex. Altogether these results show that EhCP112 is a molecule able to disrupt cell monolayers and digest proteins of the extracellular matrix and haemoglobin, and it is secreted by the trophozoites.

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“…Proteases have also been involved in E. histolytica virulence (Gadasi and Kessler, 1983;McKerrow, 1989;Keene et al, 1990;Reed et al, 1992;Tannich et al, 1992). There is experimental evidence demonstrating a direct correlation between virulence and rate of phagocytosis and protease activity (Orozco et al, 1985;Ankri et al, 1998;1999), but other reports contradict this assumption (Spice and Ackers, 1992;Montfort et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Entamoeba histolytica: a novel cysteine protease and an adhesin form the 112 kDa surface protein

Garcı́a-Rivera

Rodríguez

Ocadiz

et al. 2000

Molecular Microbiology

101

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Antisense Inhibition of Expression of Cysteine Proteinases Affects Entamoeba histolytica -Induced Formation of Liver Abscess in Hamsters

Cited by 128 publications

References 18 publications

Trigger‐induced RNAi gene silencing to identify pathogenicity factors of Entamoeba histolytica

Trigger‐induced RNAi gene silencing to identify pathogenicity factors of Entamoeba histolytica

EhCP112 is an Entamoeba histolytica secreted cysteine protease that may be involved in the parasite-virulence

Entamoeba histolytica: a novel cysteine protease and an adhesin form the 112 kDa surface protein

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