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Pore‐forming peptides of Entamoeba dispar
Author(s) -
Nickel Rosa,
Ott Claudia,
Dandekar Thomas,
Leippe Matthias
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00807.x
Subject(s) - dispar , entamoeba histolytica , biology , microbiology and biotechnology , entamoeba , lytic cycle , peptide , cytolysis , pathogen , biochemistry , virology , in vitro , cytotoxicity , virus
Amoebapore, a 77‐residue peptide with pore‐forming activity from the human pathogen Entamoeba histolytica, is implicated in the killing of phagocytosed bacteria and in the cytolytic reaction of the amoeba against host cells. Previously, we structurally and functionally characterized three amoebapore isoforms in E. histolytica but recognized only one homolog in the closely related but non‐pathogenic species Entamoeba dispar. Here, we identified two novel amoebapore homologs from E. dispar by molecular cloning. Despite strong resemblance of the primary structures of the homologs, molecular modeling predicts a species‐specific variance between the peptide structures. Parallel isolation from trophozoite extracts of the two species revealed a lower amount of pore‐forming peptides in E. dispar and substantially higher activity of the major isoform from E. histolytica towards natural membranes than that from E. dispar . Differences in abundance and activity of the lytic polypeptides may have an impact on the pathogenicity of amoebae.

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