Identification of EhICP1, a chagasin-like cysteine protease inhibitor of Entamoeba histolytica

Autor(en): Riekenberg, S
Witjes, B
Saric, M
Bruchhaus, I
Scholze, H
Stichwörter: amoebiasin; Biochemistry & Molecular Biology; Biophysics; Cell Biology; chagasin; CONSERVATION; CULTIVATION; cystatin; cysteine protease inhibitor; Entamoeba histolytica; PAPAIN; PARASITE; PATHOGENS; PROTEINASE-INHIBITOR; PROTOZOAN; RAY CRYSTAL-STRUCTURE; SEQUENCE; TRYPANOSOMA-CRUZI
Erscheinungsdatum: 2005
Herausgeber: WILEY
Journal: FEBS LETTERS
Volumen: 579
Ausgabe: 7
Startseite: 1573
Seitenende: 1578
Zusammenfassung: 
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 similar to 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 mu M) and trophozoite extract (K-i in sub-mM range), it may be a candidate for the rational development of anti-amoebiasis drugs. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
ISSN: 18733468
DOI: 10.1016/j.febslet.2005.01.067

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