ArticleEukaryotic cell2003
The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation.
Article in Eukaryotic cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 161 citations in OpenAlex.
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- Extracellular Cysteine Proteases of Key Intestinal Protozoan Pathogens-Factors Linked to Virulence and Pathogenicity.International journal of molecular sciences · 2023Review
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- Insights into the Mechanisms ofAntioxidants (Basel, Switzerland) · 2022Article
- Mucolytic bacteria: prevalence in various pathological diseases.World journal of microbiology & biotechnology · 2021Review
- The Mastigamoeba balamuthi Genome and the Nature of the Free-Living Ancestor of Entamoeba.Molecular biology and evolution · 2021Article
- Proteases as Therapeutic Targets Against the Parasitic CnidarianFrontiers in cellular and infection microbiology · 2021Article
- ArfX2 GTPase Regulates Trafficking From the Trans-Golgi to Lysosomes and Is Necessary for Liver Abscess Formation in the Protozoan ParasiteFrontiers in cellular and infection microbiology · 2021Article
- Taxon-Specific Proteins of the PathogenicFrontiers in cellular and infection microbiology · 2021Review
- Identification and biochemical characterisation of Acanthamoeba castellanii cysteine protease 3.Parasites & vectors · 2020Article
- Differential Pathogenic Gene Expression ofMicroorganisms · 2020Article
- Acetylcholine UpregulatesFrontiers in cellular and infection microbiology · 2020Article
- Review
- Genetic Diversity and Gene Family Expansions in Members of the Genus Entamoeba.Genome biology and evolution · 2019Article
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- Knockdown of Five Genes Encoding Uncharacterized Proteins Inhibits Entamoeba histolytica Phagocytosis of Dead Host Cells.Infection and immunity · 2016Article
- The Genome of Nosema sp. Isolate YNPr: A Comparative Analysis of Genome Evolution within the Nosema/Vairimorpha Clade.PloS one · 2016Article
- Infection Strategies of Intestinal Parasite Pathogens and Host Cell Responses.Frontiers in microbiology · 2016Review
- Essential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellanii.PloS one · 2015Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cysteine proteases are known to be important pathogenicity factors of the protozoan parasite Entamoeba histolytica. So far, a total of eight genes coding for cysteine proteases have been identified in E. histolytica, two of which are absent in the closely related nonpathogenic species E. dispar. However, present knowledge is restricted to enzymes expressed during in vitro cultivation of the parasite, which might represent only a subset of the entire repertoire. Taking advantage of the current E. histolytica genome-sequencing efforts, we analyzed databases containing more than 99% of all ameba gene sequences for the presence of cysteine protease genes. A total of 20 full-length genes was identified (including all eight genes previously reported), which show 10 to 86% sequence identity. The various genes obviously originated from two separate ancestors since they form two distinct clades. Despite cathepsin B-like substrate specificities, all of the ameba polypeptides are structurally related to cathepsin L-like enzymes. None of the previously described enzymes but 7 of the 12 newly identified proteins are unique compared to cathepsins of higher eukaryotes in that they are predicted to have transmembrane or glycosylphosphatidylinositol anchor attachment domains. Southern blot analysis revealed that orthologous sequences for all of the newly identified proteases are present in E. dispar. Interestingly, the majority of the various cysteine protease genes are not expressed in E. histolytica or E. dispar trophozoites during in vitro cultivation. Therefore, it is likely that at least some of these enzymes are required for infection of the human host and/or for completion of the parasite life cycle.
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