Identification of EhICP1, a chagasin-like cysteine protease inhibitor of Entamoeba histolytica
| Autor: | Henning Scholze, B. Witjes, Mirela Šarić, Iris Bruchhaus, Sabine Riekenberg |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Lysis
medicine.medical_treatment Molecular Sequence Data Biophysics Cysteine Proteinase Inhibitors Chagasin Biochemistry Homology (biology) Protein Structure Secondary law.invention chemistry.chemical_compound Entamoeba histolytica Structural Biology law Papain Genetics medicine Animals Amino Acid Sequence Molecular Biology Protease biology Amoebiasin Cystatin Cell Biology biology.organism_classification Molecular biology Cysteine protease Recombinant Proteins Cysteine Endopeptidases chemistry Recombinant DNA Cysteine protease inhibitor Sequence Alignment |
| Zdroj: | FEBS Letters. (7):1573-1578 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2005.01.067 |
| Popis: | Based on the Entamoeba histolytica genome project ( www.sanger.ac.uk/Projects/E_histolytica/ ) we have identified a cysteine protease inhibitor, EhICP1 (amoebiasin 1), with significant homology to chagasin. Recombinant EhICP1 inhibited the protease activity of papain and that of a trophozoite lysate with K i ’s in the picomolar range. By immunocytology, we localized the endogenous ∼13 kDa EhICP1 in a finely dotted subcellular distribution discrete from the vesicles containing the amoebic cysteine protease, EhCP1 (amoebapain). In an overlay assay, we observed binding of recombinant EhICP1 to EhCP1. As a heptapeptide (GNPTTGF) corresponding to the second conserved chagasin motif inhibited the protease activity of both papain ( K i 1.5 μM) and trophozoite extract ( K i in sub-mM range), it may be a candidate for the rational development of anti-amoebiasis drugs. |
| Databáze: | OpenAIRE |
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