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FEBS Lett ; 579(7): 1573-8, 2005 Mar 14.
Article in English | MEDLINE | ID: mdl-15757643

ABSTRACT

Based on the Entamoeba histolytica genome project (www.sanger.ac.uk/Project/E_histolytical/) 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 Ki's in the picomolar range. By immunocytology, we localized the endogenous approximately 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) 1.5 microM) and trophozoite extract (Ki in sub-mM range), it may be a candidate for the rational development of anti-amoebiasis drugs.


Subject(s)
Cysteine Endopeptidases/metabolism , Cysteine Proteinase Inhibitors/chemistry , Cysteine Proteinase Inhibitors/pharmacology , Entamoeba histolytica/metabolism , Amino Acid Sequence , Animals , Cysteine Endopeptidases/analysis , Cysteine Proteinase Inhibitors/metabolism , Entamoeba histolytica/chemistry , Molecular Sequence Data , Papain/antagonists & inhibitors , Protein Structure, Secondary , Recombinant Proteins/metabolism , Sequence Alignment
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